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  • Models, Molecular  (15)
  • American Association for the Advancement of Science (AAAS)  (15)
  • Springer Nature
  • 2000-2004
  • 1995-1999  (15)
  • 1980-1984
  • 1940-1944
  • 1999  (15)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (15)
  • Springer Nature
Years
  • 2000-2004
  • 1995-1999  (15)
  • 1980-1984
  • 1940-1944
Year
  • 1
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    X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-08-14
    Description: Type 1 pili-adhesive fibers expressed in most members of the Enterobacteriaceae family-mediate binding to mannose receptors on host cells through the FimH adhesin. Pilus biogenesis proceeds by way of the chaperone/usher pathway. The x-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5 angstrom resolution reveals the basis for carbohydrate recognition and for pilus assembly. The carboxyl-terminal pilin domain of FimH has an immunoglobulin-like fold, except that the seventh strand is missing, leaving part of the hydrophobic core exposed. A donor strand complementation mechanism in which the chaperone donates a strand to complete the pilin domain explains the basis for both chaperone function and pilus biogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choudhury, D -- Thompson, A -- Stojanoff, V -- Langermann, S -- Pinkner, J -- Hultgren, S J -- Knight, S D -- R01AI29549/AI/NIAID NIH HHS/ -- R01DK51406/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1999 Aug 13;285(5430):1061-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Uppsala Biomedical Center, Swedish University of Agricultural Sciences, Box 590, S-753 24 Uppsala, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10446051" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/*chemistry/metabolism ; *Adhesins, Escherichia coli ; Amino Acid Sequence ; Bacterial Outer Membrane Proteins/*chemistry/metabolism ; *Bacterial Proteins ; Chlorpropamide/analogs & derivatives/metabolism ; Crystallography, X-Ray ; Escherichia coli/*chemistry/metabolism/pathogenicity ; *Escherichia coli Proteins ; Fimbriae Proteins ; Fimbriae, Bacterial/chemistry/*metabolism/ultrastructure ; Hydrogen Bonding ; Membrane Proteins/*chemistry ; Models, Molecular ; Molecular Chaperones/*chemistry/metabolism ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Sequence Alignment
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Evolution of shape complementarity and catalytic efficiency from a primordial antibody template (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-22
    Description: The crystal structure of an efficient Diels-Alder antibody catalyst at 1.9 angstrom resolution reveals almost perfect shape complementarity with its transition state analog. Comparison with highly related progesterone and Diels-Alderase antibodies that arose from the same primordial germ line template shows the relatively subtle mutational steps that were able to evolve both structural complementarity and catalytic efficiency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, J -- Deng, Q -- Chen, J -- Houk, K N -- Bartek, J -- Hilvert, D -- Wilson, I A -- CA27489/CA/NCI NIH HHS/ -- GM38273/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Dec 17;286(5448):2345-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10600746" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Catalytic/*chemistry/genetics/*metabolism ; Binding Sites, Antibody ; Catalysis ; Chemistry, Physical ; Crystallography, X-Ray ; *Evolution, Molecular ; Haptens/chemistry/metabolism ; Hydrogen Bonding ; Immunoglobulin Fab Fragments/chemistry/metabolism ; Ligands ; Models, Molecular ; Mutation ; Physicochemical Phenomena ; Progesterone/immunology ; Protein Conformation ; Solubility ; Temperature ; Templates, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-02-12
    Description: Erythropoietin receptor (EPOR) is thought to be activated by ligand-induced homodimerization. However, structures of agonist and antagonist peptide complexes of EPOR, as well as an EPO-EPOR complex, have shown that the actual dimer configuration is critical for the biological response and signal efficiency. The crystal structure of the extracellular domain of EPOR in its unliganded form at 2.4 angstrom resolution has revealed a dimer in which the individual membrane-spanning and intracellular domains would be too far apart to permit phosphorylation by JAK2. This unliganded EPOR dimer is formed from self-association of the same key binding site residues that interact with EPO-mimetic peptide and EPO ligands. This model for a preformed dimer on the cell surface provides insights into the organization, activation, and plasticity of recognition of hematopoietic cell surface receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Livnah, O -- Stura, E A -- Middleton, S A -- Johnson, D L -- Jolliffe, L K -- Wilson, I A -- GM49497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Feb 12;283(5404):987-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9974392" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/chemistry ; Crystallography, X-Ray ; Dimerization ; Erythropoietin/metabolism ; Humans ; Hydrogen Bonding ; Janus Kinase 2 ; Ligands ; Models, Molecular ; Peptide Fragments/*chemistry/metabolism ; Peptides, Cyclic/metabolism ; Protein Conformation ; Protein-Tyrosine Kinases/metabolism ; *Proto-Oncogene Proteins ; Receptors, Erythropoietin/*chemistry/metabolism
    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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    Molecular architecture of the rotary motor in ATP synthase (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-11-27
    Description: Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits. Each c subunit forms an alpha-helical hairpin. The interhelical loops of six to seven of the c subunits are in close contact with the gamma and delta subunits of the central stalk. The extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stock, D -- Leslie, A G -- Walker, J E -- New York, N.Y. -- Science. 1999 Nov 26;286(5445):1700-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10576729" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Catalysis ; Crystallization ; Crystallography, X-Ray ; Hydrogen Bonding ; Mitochondria/enzymology ; Models, Molecular ; Molecular Motor Proteins/*chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proton-Motive Force ; Proton-Translocating ATPases/*chemistry/metabolism ; Protons ; Saccharomyces cerevisiae/enzymology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Crystal structure of the ectodomain of human transferrin receptor (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-10-26
    Description: The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome. The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit. One domain closely resembles carboxy- and aminopeptidases, and features of membrane glutamate carboxypeptidase can be deduced from the TfR structure. A model is proposed for Tf binding to the receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawrence, C M -- Ray, S -- Babyonyshev, M -- Galluser, R -- Borhani, D W -- Harrison, S C -- New York, N.Y. -- Science. 1999 Oct 22;286(5440):779-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Children's Hospital Laboratory of Molecular Medicine, 320 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10531064" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; CHO Cells ; Carboxypeptidases/chemistry ; Cell Membrane/chemistry ; Conserved Sequence ; Cricetinae ; Crystallography, X-Ray ; Dimerization ; Ferric Compounds/metabolism ; Glycosylation ; Humans ; Hydrogen-Ion Concentration ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Receptors, Transferrin/*chemistry/metabolism ; Transferrin/metabolism
    Print ISSN: 0036-8075
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  • 6
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    A glycyl radical site in the crystal structure of a class III ribonucleotide reductase (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-03-05
    Description: Ribonucleotide reductases catalyze the reduction of ribonucleotides to deoxyribonucleotides. Three classes have been identified, all using free-radical chemistry but based on different cofactors. Classes I and II have been shown to be evolutionarily related, whereas the origin of anaerobic class III has remained elusive. The structure of a class III enzyme suggests a common origin for the three classes but shows differences in the active site that can be understood on the basis of the radical-initiation system and source of reductive electrons, as well as a unique protein glycyl radical site. A possible evolutionary relationship between early deoxyribonucleotide metabolism and primary anaerobic metabolism is suggested.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Logan, D T -- Andersson, J -- Sjoberg, B M -- Nordlund, P -- New York, N.Y. -- Science. 1999 Mar 5;283(5407):1499-504.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Department of Molecular Biology, Stockholm University, S-106 91 Stockholm, Sweden. derek@biokemi.su.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10066165" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/chemistry/metabolism ; Amino Acid Sequence ; Anaerobiosis ; Binding Sites ; Crystallography, X-Ray ; Dimerization ; Evolution, Molecular ; Glycine/*chemistry ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Ribonucleotide Reductases/*chemistry/genetics/metabolism ; Viral Proteins/chemistry
    Print ISSN: 0036-8075
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  • 7
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    Structural rearrangements underlying K+-channel activation gating (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-07-03
    Description: The intramembrane molecular events underlying activation gating in the Streptomyces K+ channel were investigated by site-directed spin-labeling methods and electron paramagnetic resonance spectroscopy. A comparison of the closed and open conformations of the channel revealed periodic changes in spin-label mobility and intersubunit spin-spin interaction consistent with rigid-body movements of the two transmembrane helices TM1 and TM2. These changes involve translations and counterclockwise rotations of both helices relative to the center of symmetry of the channel. The movement of TM2 increases the diameter of the permeation pathway along the point of convergence of the four subunits, thus opening the pore. Although the extracellular residues flanking the selectivity filter remained immobile during gating, small movements were detected at the C-terminal end of the pore helix, with possible implications to the gating mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perozo, E -- Cortes, D M -- Cuello, L G -- GM54690/GM/NIGMS NIH HHS/ -- GM57846/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Jul 2;285(5424):73-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Physiology and Biological Physics and Center for Structural Biology, University of Virginia Health Sciences Center, Charlottesville, VA 22906-0011, USA. eperozo@virginia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10390363" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacterial Proteins ; Binding Sites ; Circular Dichroism ; Cysteine/chemistry ; Electron Spin Resonance Spectroscopy ; Hydrogen-Ion Concentration ; *Ion Channel Gating ; Models, Molecular ; Potassium/*metabolism ; Potassium Channels/*chemistry/*physiology ; Protein Conformation ; Protein Structure, Secondary ; Rubidium/metabolism ; Sequence Deletion ; Streptomyces/chemistry/physiology
    Print ISSN: 0036-8075
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  • 8
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    Oligomeric structure of the human EphB2 receptor SAM domain (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-02-05
    Description: The sterile alpha motif (SAM) domain is a protein interaction module that is present in diverse signal-transducing proteins. SAM domains are known to form homo- and hetero-oligomers. The crystal structure of the SAM domain from an Eph receptor tyrosine kinase, EphB2, reveals two large interfaces. In one interface, adjacent monomers exchange amino-terminal peptides that insert into a hydrophobic groove on each neighbor. A second interface is composed of the carboxyl-terminal helix and a nearby loop. A possible oligomer, constructed from a combination of these binding modes, may provide a platform for the formation of larger protein complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thanos, C D -- Goodwill, K E -- Bowie, J U -- New York, N.Y. -- Science. 1999 Feb 5;283(5403):833-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UCLA-DOE Laboratory of Structural Biology and Molecular Medicine and Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9933164" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallization ; Crystallography, X-Ray ; Dimerization ; GRB10 Adaptor Protein ; Humans ; Hydrogen Bonding ; Kinesin/metabolism ; Models, Molecular ; Myosins/metabolism ; Phosphorylation ; *Protein Conformation ; Protein Structure, Secondary ; Protein Tyrosine Phosphatases/metabolism ; Proteins/metabolism ; Receptor Aggregation ; Receptor Protein-Tyrosine Kinases/*chemistry/metabolism ; Receptor, EphB2 ; Recombinant Proteins/chemistry/metabolism ; Surface Properties
    Print ISSN: 0036-8075
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  • 9
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    Crystal structure of a conserved ribosomal protein-RNA complex (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-05-15
    Description: The structure of a highly conserved complex between a 58-nucleotide domain of large subunit ribosomal RNA and the RNA-binding domain of ribosomal protein L11 has been solved at 2.8 angstrom resolution. It reveals a precisely folded RNA structure that is stabilized by extensive tertiary contacts and contains an unusually large core of stacked bases. A bulge loop base from one hairpin of the RNA is intercalated into the distorted major groove of another helix; the protein locks this tertiary interaction into place by binding to the intercalated base from the minor groove side. This direct interaction with a key ribosomal RNA tertiary interaction suggests that part of the role of L11 is to stabilize an unusual RNA fold within the ribosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Conn, G L -- Draper, D E -- Lattman, E E -- Gittis, A G -- R37 GM29048/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 May 14;284(5417):1171-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10325228" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/metabolism ; Base Pairing ; Base Sequence ; Binding Sites ; Crystallography, X-Ray ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Peptide Elongation Factor G ; Peptide Elongation Factors/metabolism ; Phylogeny ; Protein Conformation ; RNA, Bacterial/*chemistry/metabolism ; RNA, Ribosomal/*chemistry/metabolism ; Ribosomal Proteins/*chemistry/metabolism
    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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  • 10
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    How chaperones protect virgin proteins (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-09-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eisenberg, D -- New York, N.Y. -- Science. 1999 Aug 13;285(5430):1021-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉DOE Laboratory of Structural Biology and Molecular Medicine, University of California, Los Angeles, CA 90095, USA. david@mbi.ucla.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10475844" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/chemistry/metabolism ; *Adhesins, Escherichia coli ; Bacterial Outer Membrane Proteins/chemistry/metabolism ; Bacterial Proteins/chemistry/*metabolism ; Crystallography, X-Ray ; Escherichia coli/metabolism/ultrastructure ; *Escherichia coli Proteins ; Fimbriae Proteins ; Fimbriae, Bacterial/*metabolism/ultrastructure ; Membrane Proteins/chemistry/*metabolism ; Models, Molecular ; Molecular Chaperones/*chemistry/*metabolism ; *Periplasmic Proteins ; Protein Folding ; Protein Structure, Secondary ; Thermodynamics
    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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