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1vr8

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

    Title Crystal structure of an ORFan protein (TM1622) from Thermotoga maritima at 1.75 A resolution reveals a fold similar to the Ran-binding protein Mog1p. Proteins 65 777-782 2006
    Site JCSG
    PDB Id 1vr8 Target Id 358480
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1395,TM1622 Molecular Weight 15125.72 Da.
    Residues 130 Isoelectric Point 8.77
    Sequence ppeaysldtaifvletrdyrlsdvkeidsygdvemkgkvavfeteygpvflyvykgeeakkiwkklngr agfvsirsvldlpnmgkfstvsngkkivawwrknwlfivegkngveefvkhvyrvyeemkq
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.75 Rfree 0.18179
    Matthews' coefficent 2.32 Rfactor 0.1486
    Waters 172 Solvent Content 46.46

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1vr8
    1. The Buccaneer software for automated model building. 1. Tracing protein chains
    K Cowtan - Acta Crystallographica Section D: Biological , 2006 - scripts.iucr.org
     
    2. Insights into proteinprotein interfaces using a Bayesian network prediction method
    JR Bradford, CJ Needham, AJ Bulpitt - Journal of molecular , 2006 - Elsevier
     
    3. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard
    TC Terwilliger, PD Adams, RJ Read - Section D: Biological , 2009 - scripts.iucr.org
     
    4. The structure of RseB: a sensor in periplasmic stress response of E. coli
    P Wollmann, K Zeth - Journal of molecular biology, 2007 - Elsevier
     
    5. Autoindexing with outlier rejection and identification of superimposed lattices
    NK Sauter, BK Poon - Journal of Applied Crystallography, 2010 - scripts.iucr.org
     
    6. Crystal structure of an ORFan protein (TM1622) from Thermotoga maritima at 1.75 resolution reveals a fold similar to the Ran_binding protein Mog1p
    Q Xu, S Krishna, D McMullan - Proteins: Structure, , 2006 - Wiley Online Library
     
    7. Structure and ligand binding of the soluble domain of a Thermotoga maritima membrane protein of unknown function TM1634
    CJ McCleverty, L Columbus, A Kreusch - Protein , 2008 - Wiley Online Library
     
    8. Structure of the Sensor Domain of Mycobacterium tuberculosis PknH Receptor Kinase Reveals a Conserved Binding Cleft
    A Cavazos, DM Prigozhin, T Alber - Journal of Molecular Biology, 2012 - Elsevier
     
    9. The Structure of RseB, a Sensor for Periplasmic Stress in Escherichia coli
    P Wollmann - 2008 - edoc.ub.uni-muenchen.de
     

    Protein Summary

    Crystal structure of TM1622 from Thermotoga maritima has uniq structure and sequence. TM1622 fold resembles fold of Ran-binding protein Mog1p, but lacks a characteristic N-terminal ?-hairpin.

    PFP server identified TM1622 as"Rab GTPase binding" (GO:0017137; PubMed:16672240).

    Ligand Summary



    References

    Reviews

    References

     

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