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1vq0

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

    Title Crystal structure of Hsp33 chaperone (TM1394) from Thermotoga maritima at 2.20 A resolution. Proteins 61 669-673 2005
    Site JCSG
    PDB Id 1vq0 Target Id 283255
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1285,TM1394, 89982 Molecular Weight 32538.84 Da.
    Residues 290 Isoelectric Point 5.33
    Sequence miyygtmfdhkvrfsivrmrevveearnrhalsylatvvlgraligaalvtpwlaekerwtldiegngp irrvvaqstseftvrgyvanpkvelplnekgkfdvagaigqgvlrvvrdlglktpfvsqvplvsgeiae dlayyfavseqipsafsigvlvdsdgvkiaggfavqiidrtleqekvemiekniknlpsisklfqeaep ldvlerifgekvgfvetaeikykcdcnrekaknallvldkkeledmrkegkgevvckwcntryvfseee leellkfkvddsgs
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.20 Rfree 0.24079
    Matthews' coefficent 3.22 Rfactor 0.19824
    Waters 273 Solvent Content 61.47

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    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1vq0
    1. Contribution of Electrostatic Interactions, Compactness and Quaternary Structure to Protein Thermostability: Lessons from Structural Genomics of Thermotoga
    M Robinson-Rechavi, A Alibs, A Godzik - Journal of molecular biology, 2006 - Elsevier
     
    2. Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species
    SB Conners, EF Mongodin, MR Johnson - FEMS microbiology , 2006 - Wiley Online Library
     
    3. The JCSG MR pipeline: optimized alignments, multiple models and parallel searches
    R Schwarzenbacher, A Godzik - Section D: Biological , 2007 - scripts.iucr.org
     
    4. Data processing and analysis with the autoPROC toolbox
    C Vonrhein, C Flensburg, P Keller, A Sharff - Section D: Biological , 2011 - scripts.iucr.org
     
    5. Structural and biochemical bases for the redox sensitivity of Mycobacterium tuberculosis RslA
    KG Thakur, T Praveena, B Gopal - Journal of molecular biology, 2010 - Elsevier
     
    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. Cyclic Peptides Bearing a Side_Chain Tail: A Tool to Model the Structure and Reactivity of Protein Zinc Sites
    O Snque, E Bourls, V Lebrun, E Bonnet - Angewandte , 2008 - Wiley Online Library
     
    8. ROS-Mediated Signalling in Bacteria: Zinc-Containing Cys-XX-Cys Redox Centres and Iron-Based Oxidative Stress
    DO de Oru Lucana, I Wedderhoff - Journal of Signal , 2012 - downloads.hindawi.com
     
    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. Carbohydrate utilization pathway analysis in the hyperthermophile Thermotoga maritima
    SB Conners - 2006 - repository.lib.ncsu.edu
     
    11. ROS-Mediated Signalling in Bacteria: Zinc-Containing Cys-XX-Cys Redox Centres and Iron-Based Oxidative Stress
    W Ina, R Matthew - Journal of Signal Transduction, 2011 - hindawi.com
     

    Protein Summary

    The TM1394 gene of Thermotoga maritima encodes a heat shock protein 33 (Hsp33).

    In normal (reducing) cytosolic conditions, four conserved Cys residues coordinate Zn ion. Under oxidative stress (such as heat shock), the Cys are reversibly oxidized to disulfide bonds, which causes the Hsp33 proteins to dimerise and to activate its chaperone activity and the ability to bind protein substrates.

    Ligand Summary



    References

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