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  • Articles  (14)
  • Protein Structure, Secondary  (14)
  • 1995-1999  (14)
  • 1998  (14)
  • Science. 278(5345): 1966-8.  (1)
  • Science. 279(5353): 1037-41.  (1)
  • Science. 279(5358): 1950-4.  (1)
  • Science. 279(5358): 1958-61.  (1)
  • Science. 279(5359): 2121-6.  (1)
  • Science. 280(5360): 69-77.  (1)
  • Science. 280(5363): 578-82.  (1)
  • Science. 280(5364): 752-5.  (1)
  • Science. 280(5367): 1277-81.  (1)
  • Science. 280(5370): 1747-9.  (1)
  • Science. 280(5371): 1949-53.  (1)
  • Science. 282(5392): 1327-32.  (1)
  • Science. 282(5397): 2215-20.  (1)
  • Science. 282(5397): 2220-6.  (1)
  • 25
  • Natural Sciences in General  (14)
  • Physics  (14)
Collection
  • Articles  (14)
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  • 1995-1999  (14)
Year
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  • 1
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    Structure of nitric oxide synthase oxygenase dimer with pterin and substrate (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: Crystal structures of the murine cytokine-inducible nitric oxide synthase oxygenase dimer with active-center water molecules, the substrate L-arginine (L-Arg), or product analog thiocitrulline reveal how dimerization, cofactor tetrahydrobiopterin, and L-Arg binding complete the catalytic center for synthesis of the essential biological signal and cytotoxin nitric oxide. Pterin binding refolds the central interface region, recruits new structural elements, creates a 30 angstrom deep active-center channel, and causes a 35 degrees helical tilt to expose a heme edge and the adjacent residue tryptophan-366 for likely reductase domain interactions and caveolin inhibition. Heme propionate interactions with pterin and L-Arg suggest that pterin has electronic influences on heme-bound oxygen. L-Arginine binds to glutamic acid-371 and stacks with heme in an otherwise hydrophobic pocket to aid activation of heme-bound oxygen by direct proton donation and thereby differentiate the two chemical steps of nitric oxide synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crane, B R -- Arvai, A S -- Ghosh, D K -- Wu, C -- Getzoff, E D -- Stuehr, D J -- Tainer, J A -- HL58883/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1998 Mar 27;279(5359):2121-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9516116" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arginine/chemistry/*metabolism ; Binding Sites ; Biopterin/*analogs & derivatives/chemistry/metabolism ; Citrulline/analogs & derivatives/chemistry/metabolism ; Crystallography, X-Ray ; Dimerization ; Hydrogen Bonding ; Isoenzymes/chemistry/metabolism ; Ligands ; Macrophages/enzymology ; Mice ; Models, Molecular ; Nitric Oxide/biosynthesis ; Nitric Oxide Synthase/*chemistry/metabolism ; Nitric Oxide Synthase Type II ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Thiourea/analogs & derivatives/chemistry/metabolism
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  • 2
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    A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-25
    Description: The entry of primate immunodeficiency viruses into target cells depends on a sequential interaction of the gp120 envelope glycoprotein with the cellular receptors, CD4 and members of the chemokine receptor family. The gp120 third variable (V3) loop has been implicated in chemokine receptor binding, but the use of the CCR5 chemokine receptor by diverse primate immunodeficiency viruses suggests the involvement of an additional, conserved gp120 element. Through the use of gp120 mutants, a highly conserved gp120 structure was shown to be critical for CCR5 binding. This structure is located adjacent to the V3 loop and contains neutralization epitopes induced by CD4 binding. This conserved element may be a useful target for pharmacologic or prophylactic intervention in human immunodeficiency virus (HIV) infections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rizzuto, C D -- Wyatt, R -- Hernandez-Ramos, N -- Sun, Y -- Kwong, P D -- Hendrickson, W A -- Sodroski, J -- AI 40895/AI/NIAID NIH HHS/ -- AI 41851/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 19;280(5371):1949-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9632396" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Antigens, CD4/metabolism ; Binding Sites ; Crystallization ; HIV Antibodies/immunology ; HIV Envelope Protein gp120/*chemistry/genetics/immunology/*metabolism ; HIV-1/*chemistry/immunology ; Humans ; Models, Molecular ; Peptide Fragments/chemistry ; Protein Conformation ; Protein Structure, Secondary ; Receptors, CCR5/*metabolism ; Recombinant Proteins/metabolism
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  • 3
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    Redesigning enzyme topology by directed evolution (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: Genetic selection was exploited in combination with structure-based design to transform an intimately entwined, dimeric chorismate mutase into a monomeric, four-helix-bundle protein with near native activity. Successful reengineering depended on choosing a thermostable starting protein, introducing point mutations that preferentially destabilize the wild-type dimer, and using directed evolution to optimize an inserted interhelical turn. Contrary to expectations based on studies of other four-helix-bundle proteins, only a small fraction of possible turn sequences (fewer than 0.05 percent) yielded well-behaved, monomeric, and highly active enzymes. Selection for catalytic function thus provides an efficient yet stringent method for rapidly assessing correctly folded polypeptides and may prove generally useful for protein design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacBeath, G -- Kast, P -- Hilvert, D -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1958-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Scripps Research Institute, Department of Chemistry, 10550 North Torrey Pines Road, La Jolla, California, 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9506949" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Catalysis ; Chorismate Mutase/*chemistry/genetics/*metabolism ; Circular Dichroism ; Cloning, Molecular ; Dimerization ; *Directed Molecular Evolution ; Escherichia coli/genetics ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; *Protein Engineering ; Protein Folding ; Protein Structure, Secondary ; Recombinant Proteins/chemistry/metabolism ; Transformation, Bacterial
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    A structural explanation for the recognition of tyrosine-based endocytotic signals (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-13
    Description: Many cell surface proteins are marked for endocytosis by a cytoplasmic sequence motif, tyrosine-X-X-(hydrophobic residue), that is recognized by the mu2 subunit of AP2 adaptors. Crystal structures of the internalization signal binding domain of mu2 complexed with the internalization signal peptides of epidermal growth factor receptor and the trans-Golgi network protein TGN38 have been determined at 2.7 angstrom resolution. The signal peptides adopted an extended conformation rather than the expected tight turn. Specificity was conferred by hydrophobic pockets that bind the tyrosine and leucine in the peptide. In the crystal, the protein forms dimers that could increase the strength and specificity of binding to dimeric receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Owen, D J -- Evans, P R -- New York, N.Y. -- Science. 1998 Nov 13;282(5392):1327-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9812899" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Protein Complex 1 ; Adaptor Protein Complex 2 ; *Adaptor Protein Complex 3 ; Adaptor Protein Complex alpha Subunits ; *Adaptor Protein Complex mu Subunits ; Adaptor Proteins, Vesicular Transport ; Amino Acid Sequence ; Animals ; Binding Sites ; Crystallography, X-Ray ; Dimerization ; *Endocytosis ; *Glycoproteins ; Humans ; Hydrogen Bonding ; Membrane Glycoproteins/*chemistry/metabolism ; Membrane Proteins/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Phosphorylation ; Protein Conformation ; Protein Sorting Signals/*chemistry/metabolism ; Protein Structure, Secondary ; Receptor, Epidermal Growth Factor/*chemistry/metabolism ; Tyrosine/chemistry/metabolism
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  • 5
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    Ribonuclease P protein structure: evolutionary origins in the translational apparatus (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: The crystal structure of Bacillus subtilis ribonuclease P protein is reported at 2.6 angstroms resolution. This protein binds to ribonuclease P RNA to form a ribonucleoprotein holoenzyme with optimal catalytic activity. Mutagenesis and biochemical data indicate that an unusual left-handed betaalphabeta crossover connection and a large central cleft in the protein form conserved RNA binding sites; a metal binding loop may comprise a third RNA binding site. The unusual topology is partly shared with ribosomal protein S5 and the ribosomal translocase elongation factor G, which suggests evolution from a common RNA binding ancestor in the primordial translational apparatus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stams, T -- Niranjanakumari, S -- Fierke, C A -- Christianson, D W -- GM55387/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 May 1;280(5364):752-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Roy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104-6323, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9563955" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/enzymology ; Binding Sites ; Catalysis ; Crystallography, X-Ray ; Endoribonucleases/*chemistry/metabolism ; *Evolution, Molecular ; Magnesium/metabolism ; Models, Molecular ; Peptide Elongation Factor G ; Peptide Elongation Factors/chemistry ; *Protein Biosynthesis ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; RNA, Bacterial/*chemistry/metabolism ; RNA, Catalytic/*chemistry/metabolism ; Ribonuclease P ; Ribosomal Proteins/chemistry ; Zinc/metabolism
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  • 6
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    Enzyme structure with two catalytic sites for double-sieve selection of substrate (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-09
    Description: High-fidelity transfers of genetic information in the central dogma can be achieved by a reaction called editing. The crystal structure of an enzyme with editing activity in translation is presented here at 2.5 angstroms resolution. The enzyme, isoleucyl-transfer RNA synthetase, activates not only the cognate substrate L-isoleucine but also the minimally distinct L-valine in the first, aminoacylation step. Then, in a second, "editing" step, the synthetase itself rapidly hydrolyzes only the valylated products. For this two-step substrate selection, a "double-sieve" mechanism has already been proposed. The present crystal structures of the synthetase in complexes with L-isoleucine and L-valine demonstrate that the first sieve is on the aminoacylation domain containing the Rossmann fold, whereas the second, editing sieve exists on a globular beta-barrel domain that protrudes from the aminoacylation domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nureki, O -- Vassylyev, D G -- Tateno, M -- Shimada, A -- Nakama, T -- Fukai, S -- Konno, M -- Hendrickson, T L -- Schimmel, P -- Yokoyama, S -- GM15539/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Apr 24;280(5363):578-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9554847" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Monophosphate ; Binding Sites ; Crystallography, X-Ray ; Escherichia coli/enzymology ; Hydrogen Bonding ; Hydrolysis ; Isoleucine/*metabolism ; Isoleucine-tRNA Ligase/*chemistry/metabolism ; Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; RNA, Transfer, Ile/metabolism ; Substrate Specificity ; Thermus thermophilus/enzymology ; Transfer RNA Aminoacylation ; Valine/*metabolism
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  • 7
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    Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-18
    Description: Mechanosensitive ion channels play a critical role in transducing physical stresses at the cell membrane into an electrochemical response. The MscL family of large-conductance mechanosensitive channels is widely distributed among prokaryotes and may participate in the regulation of osmotic pressure changes within the cell. In an effort to better understand the structural basis for the function of these channels, the structure of the MscL homolog from Mycobacterium tuberculosis was determined by x-ray crystallography to 3.5 angstroms resolution. This channel is organized as a homopentamer, with each subunit containing two transmembrane alpha helices and a third cytoplasmic alpha helix. From the extracellular side, a water-filled opening approximately 18 angstroms in diameter leads into a pore lined with hydrophilic residues which narrows at the cytoplasmic side to an occluded hydrophobic apex that may act as the channel gate. This structure may serve as a model for other mechanosensitive channels, as well as the broader class of pentameric ligand-gated ion channels exemplified by the nicotinic acetylcholine receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, G -- Spencer, R H -- Lee, A T -- Barclay, M T -- Rees, D C -- GM18486/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Dec 18;282(5397):2220-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9856938" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Cell Membrane/chemistry ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray ; *Escherichia coli Proteins ; *Ion Channel Gating ; Ion Channels/*chemistry/metabolism ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Mycobacterium tuberculosis/*chemistry ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Temperature
    Print ISSN: 0036-8075
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  • 8
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    Hormone-dependent coactivator binding to a hydrophobic cleft on nuclear receptors (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: The ligand-binding domain of nuclear receptors contains a transcriptional activation function (AF-2) that mediates hormone-dependent binding of coactivator proteins. Scanning surface mutagenesis on the human thyroid hormone receptor was performed to define the site that binds the coactivators, glucocorticoid receptor-interacting protein 1 (GRIP1) and steroid receptor coactivator 1 (SRC-1). The residues involved encircle a small surface that contains a hydrophobic cleft. Ligand activation of transcription involves formation of this surface by folding the carboxyl-terminal alpha helix against a scaffold of three other helices. These features may represent general ones for nuclear receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, W -- Ribeiro, R C -- Wagner, R L -- Nguyen, H -- Apriletti, J W -- Fletterick, R J -- Baxter, J D -- Kushner, P J -- West, B L -- DK09516/DK/NIDDK NIH HHS/ -- DK51281/DK/NIDDK NIH HHS/ -- P41-RR01081/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 12;280(5370):1747-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Metabolic Research Unit, Box 0540, University of California San Francisco, San Francisco, CA 94143-0540, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9624051" target="_blank"〉PubMed〈/a〉
    Keywords: HeLa Cells ; Histone Acetyltransferases ; Humans ; Ligands ; Models, Molecular ; Mutagenesis, Site-Directed ; Nuclear Receptor Coactivator 1 ; Nuclear Receptor Coactivator 2 ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Receptors, Retinoic Acid/metabolism ; Receptors, Thyroid Hormone/*chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Retinoid X Receptors ; Transcription Factors/*metabolism ; *Transcriptional Activation ; Triiodothyronine/*metabolism/pharmacology
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  • 9
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    Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-18
    Description: FhuA, the receptor for ferrichrome-iron in Escherichia coli, is a member of a family of integral outer membrane proteins, which, together with the energy-transducing protein TonB, mediate the active transport of ferric siderophores across the outer membrane of Gram-negative bacteria. The three-dimensional structure of FhuA is presented here in two conformations: with and without ferrichrome-iron at resolutions of 2.7 and 2.5 angstroms, respectively. FhuA is a beta barrel composed of 22 antiparallel beta strands. In contrast to the typical trimeric arrangement found in porins, FhuA is monomeric. Located within the beta barrel is a structurally distinct domain, the "cork," which mainly consists of a four-stranded beta sheet and four short alpha helices. A single lipopolysaccharide molecule is noncovalently associated with the membrane-embedded region of the protein. Upon binding of ferrichrome-iron, conformational changes are transduced to the periplasmic pocket of FhuA, signaling the ligand-loaded status of the receptor. Sequence homologies and mutagenesis data are used to propose a structural mechanism for TonB-dependent siderophore-mediated transport across the outer membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferguson, A D -- Hofmann, E -- Coulton, J W -- Diederichs, K -- Welte, W -- New York, N.Y. -- Science. 1998 Dec 18;282(5397):2215-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, McGill University, 3775 University Street, Montreal, Quebec, Canada H3A 2B4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9856937" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Outer Membrane Proteins/*chemistry/metabolism ; Bacterial Proteins/chemistry/metabolism ; Binding Sites ; Biological Transport, Active ; Cell Membrane/chemistry/metabolism ; Crystallography, X-Ray ; Diffusion ; Escherichia coli/*chemistry/metabolism ; *Escherichia coli Proteins ; Ferric Compounds/*metabolism ; Ferrichrome/*metabolism ; Hydrogen Bonding ; Ligands ; Lipopolysaccharides/*metabolism ; Membrane Proteins/chemistry/metabolism ; Models, Molecular ; *Protein Conformation ; Protein Structure, Secondary ; Receptors, Virus/*chemistry/metabolism ; Signal Transduction
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  • 10
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    The structure of the potassium channel: molecular basis of K+ conduction and selectivity (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-29
    Description: The potassium channel from Streptomyces lividans is an integral membrane protein with sequence similarity to all known K+ channels, particularly in the pore region. X-ray analysis with data to 3.2 angstroms reveals that four identical subunits create an inverted teepee, or cone, cradling the selectivity filter of the pore in its outer end. The narrow selectivity filter is only 12 angstroms long, whereas the remainder of the pore is wider and lined with hydrophobic amino acids. A large water-filled cavity and helix dipoles are positioned so as to overcome electrostatic destabilization of an ion in the pore at the center of the bilayer. Main chain carbonyl oxygen atoms from the K+ channel signature sequence line the selectivity filter, which is held open by structural constraints to coordinate K+ ions but not smaller Na+ ions. The selectivity filter contains two K+ ions about 7.5 angstroms apart. This configuration promotes ion conduction by exploiting electrostatic repulsive forces to overcome attractive forces between K+ ions and the selectivity filter. The architecture of the pore establishes the physical principles underlying selective K+ conduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doyle, D A -- Morais Cabral, J -- Pfuetzner, R A -- Kuo, A -- Gulbis, J M -- Cohen, S L -- Chait, B T -- MacKinnon, R -- New York, N.Y. -- Science. 1998 Apr 3;280(5360):69-77.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neurobiology and Biophysics and the Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9525859" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Bacterial Proteins ; Binding Sites ; Cesium/metabolism ; Crystallization ; Crystallography, X-Ray ; Fourier Analysis ; Hydrogen Bonding ; Lipid Bilayers ; Models, Molecular ; Molecular Sequence Data ; Potassium/*metabolism ; Potassium Channel Blockers ; Potassium Channels/*chemistry/*metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Rubidium/metabolism ; Scorpion Venoms/metabolism/pharmacology ; Sodium/metabolism ; Static Electricity ; Streptomyces/chemistry ; Tetraethylammonium/metabolism/pharmacology ; Water
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