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  • Crystallography  (2)
  • American Association for the Advancement of Science (AAAS)  (1)
  • Springer  (1)
  • American Society of Hematology
  • Deutsches GeoForschungsZentrum GFZ
  • Oxford University Press
  • 2000-2004  (2)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (1)
  • Springer  (1)
  • American Society of Hematology
  • Deutsches GeoForschungsZentrum GFZ
  • Oxford University Press
Years
  • 2000-2004  (2)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Three-Dimensional Structure of Nucleoside Diphosphate Kinase (2000)
    Springer
    Journal of bioenergetics and biomembranes 32 (2000), S. 215-225 
    Details
    ISSN: 1573-6881
    Keywords: Crystallography ; ferredoxin fold ; quaternary structure ; nucleotide binding ; transition state analog ; substrate-assisted catalysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Three-dimensional structures are known from X-ray studies of the nucleoside diphosphate(NDP) kinase of many organisms from bacteria to human. All NDP kinases have subunits ofabout 150 residues with a very similar fold based on the αβ sandwich orferredoxin fold.This fold is found in many nucleotide or polynucleotide-binding proteins with no sequencerelationship to NDP kinase. This common fold is augmented here with specificfeatures: asurface α-helix hairpin, the Kpn loop, and the C-terminal extension. The α-helix hairpin andKpn loop make up the nucleotide binding site, which is unique to NDP kinase and differentfrom that of other kinases or ATPases. The Kpn loop and the C-terminal extension are alsoinvolved in the quaternary structure. Whereas all known eukaryotic NDP kinases, includingmitochondral enzymes, are hexamers, some bacterial enzymes are tetramers. However,hexameric and tetrameric NDP kinases are built from the same dimer. The structural environmentof the active histidine is identical in all. The nucleotide binding site is also fully conserved,except for a feature implicating C-terminal residues in the hexamer, but not in the tetramer.Structural data on the native and phosphorylated enzyme, complexes with substrates, inhibitor,and a transition state analog, give a solid basis to a mechanism of phosphate transfer in whichthe largest contributors to catalysis are the 3′-OH of the sugar and the bound Mg2+ in thenucleotide substrate. In contrast, we still lack structural data relating to DNA binding andother functions of NDP kinases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005528811303
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    Paper (German National Licenses)
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  • 2
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    A linear, O-coordinated eta1-CO2 bound to uranium (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-18
    Description: The electron-rich, six-coordinate tris-aryloxide uranium(III) complex [((AdArO)3tacn)U(III)] [where (AdArOH)3tacn = 1,4,7-tris(3-adamantyl-5-tert-butyl-2-hydroxybenzyl)1,4,7-triazacyclononane] reacts rapidly with CO2 to yield [((AdArO)3tacn)U(IV)(CO2)], a complex in which the CO(2) ligand is linearly coordinated to the metal through its oxygen atom (eta1-OCO). The latter complex has been crystallographically and spectroscopically characterized. The inequivalent O-C-O bond lengths [1.122 angstroms (A) for the O-C bond adjacent to uranium and 1.277 A for the other], considered together with magnetization data and electronic and vibrational spectra, support the following bonding model: U(IV)=O=C*-O- 〈--〉 U(IV)-OC-O-. In these charge-separated resonance structures, the uranium center is oxidized to uranium(IV) and the CO2 ligand reduced by one electron.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castro-Rodriguez, Ingrid -- Nakai, Hidetaka -- Zakharov, Lev N -- Rheingold, Arnold L -- Meyer, Karsten -- 3 T32 DK07233-2651/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2004 Sep 17;305(5691):1757-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, MC 0358, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15375263" target="_blank"〉PubMed〈/a〉
    Keywords: Carbon Dioxide/*chemistry ; Crystallography ; Electrons ; Hydrophobic and Hydrophilic Interactions ; Ligands ; Magnetics ; Models, Molecular ; Molecular Structure ; Oxidation-Reduction ; Oxygen/*chemistry ; Spectrum Analysis ; Temperature ; Uranium/*chemistry ; X-Rays
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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