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    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 APC1014
    Molecular Characteristics
    Source Bacillus subtilis
    Alias Ids TPS4481,P37565, 1423 Molecular Weight 31809.55 Da.
    Residues 291 Isoelectric Point 4.85
    Sequence mdylvkalaydgkvrayaarttdmvnegqrrhgtwptasaalgrtmtaslmlgamlkgddkltvkiegg gpigaivadanakgevrayvsnpqvhfdlneqgkldvrravgtngtlsvvkdlglrefftgqveivsge lgddftyylvsseqvpssvgvgvlvnpdntilaaggfiiqlmpgtddetitkieqrlsqvepiskliqk gltpeeileevlgekpeiletmpvrfhcpcskerfetailglgkkeiqdmieedgqaeavchfcnekyl ftkeeleglrdqttr
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.97 Rfree 0.225
    Matthews' coefficent 3.2 Rfactor 0.197
    Waters 277 Solvent Content 61.4

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


    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
    NI Nicely, D Parsonage, C Paige - of unique coenzyme , 2008 - books.google.com

    Protein Summary

    Ligand Summary




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