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1vzy

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary

    Title The Crystal Structure of the Reduced, Zn(2+)-Bound Form of the B. Subtilis Hsp33 Chaperone and its Implications for the Activation Mechanism. Structure 12 1901 2004
    Site MCSG
    PDB Id 1vzy Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS4481,P37565, 1423
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 3.2 Rfactor 0.197
    Waters
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    Solvent Content 61.4

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    Ligand Information
    Ligands ACT (ACETATE) x 6
    Metals ZN (ZINC) x 2

    Jmol

     
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    Google Scholar output for 1vzy
    1. Entropy and surface engineering in protein crystallization
    ZS Derewenda, PG Vekilov - Acta Crystallographica Section D: , 2005 - scripts.iucr.org
     
    2. Towards fully automated structure-based function prediction in structural genomics: a case study
    JD Watson, S Sanderson, A Ezersky - Journal of molecular , 2007 - Elsevier
     
    3. The redox-switch domain of Hsp33 functions as dual stress sensor
    M Ilbert, J Horst, S Ahrens, J Winter, PCF Graf - Nature structural & , 2007 - nature.com
     
    4. The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism
    I Janda, Y Devedjiev, U Derewenda, Z Dauter - Structure, 2004 - Elsevier
     
    5. Prediction of transition metal_binding sites from apo protein structures
    M Babor, S Gerzon, B Raveh - Proteins: Structure, , 2008 - Wiley Online Library
     
    6. Crystal structure of Hsp33 chaperone (TM1394) from Thermotoga maritima at 2.20 resolution
    L Jaroszewski, R Schwarzenbacher - Proteins: Structure, , 2005 - Wiley Online Library
     
    7. Unfolding of Metastable Linker Region Is at the Core of Hsp33 Activation as a Redox-regulated Chaperone
    CM Cremers, D Reichmann, J Hausmann - Journal of Biological , 2010 - ASBMB
     
    8. Minimal Functional Sites Allow a Classification of Zinc Sites in Proteins
    C Andreini, I Bertini, G Cavallaro - PloS one, 2011 - dx.plos.org
     
    9. Crystal structure of constitutively monomeric E. coli Hsp33 mutant with chaperone activity
    SW Chi, DG Jeong, JR Woo, HS Lee, BC Park, BY Kim - FEBS letters, 2011 - Elsevier
     
    10. The Unfolding Story of a Redox Chaperone
    MP Mayer - Cell, 2012 - Elsevier
     
    11. Oxidation-Induced Conformational Change of a Prokaryotic Molecular Chaperone, Hsp33, Monitored by Selective Isotope Labeling
    YS Lee, KS Ryu, Y Lee, S Kim, KW Lee - Journal of the Korean , 2011 - bio.gnu.kr
     
    12. Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution
    YS Lee, KS Ryu, SJ Kim, HS Ko, DW Sim, YH Jeon - FEBS letters, 2012 - Elsevier
     
    13. DEPENDENT REDOX BIOLOGY
    NI Nicely, D Parsonage, C Paige - of unique coenzyme , 2008 - books.google.com
     

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    Protein Summary


    Ligand Summary

    Reviews

    References

     

    No references found.

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