The Open Protein Structure Annotation Network
PDB Keyword


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

    Title Crystal structure of Periplasmic divalent cation tolerance protein (TM1056) from Thermotoga maritima at 1.95 A resolution. To be published
    Site JCSG
    PDB Id 1o5j Target Id 282923
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1257,TM1056, 84666 Molecular Weight 12176.50 Da.
    Residues 101 Isoelectric Point 5.30
    Sequence milvystfpneekaleigrkllekrliacfnafeirsgywwkgeivqdkewaaifktteekekelyeel rklhpyetpaiftlkvenvlteymnwlresvl
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.95 Rfree 0.22061
    Matthews' coefficent 2.05 Rfactor 0.15603
    Waters 74 Solvent Content 39.45

    Access denied for user 'root'@'localhost' (using password: YES) (click for details)

    Ligand Information


    Google Scholar output for 1o5j
    1. Structural analysis of a set of proteins resulting from a bacterial genomics project
    J Badger, JM Sauder, JM Adams - Proteins: Structure, , 2005 - Wiley Online Library
    2. Shotgun crystallization strategy for structural genomics II: crystallization conditions that produce high resolution structures for T. maritima proteins
    R Page, AM Deacon, SA Lesley - Journal of structural and , 2005 - Springer
    3. Protein structural classification and family identification by multifractal analysis and wavelet spectrum
    SM Zhu, ZG Yu, A Vo - Chinese Physics B, 2011 - iopscience.iop.org

    Protein Summary

    The gene TM1056 from Thermotoga maritima encodes a protein CutA (CutA1 superfamily) involved in divalent metal tolerance PF03091 .  The structure of Thermotoga CutA has been solved previously 1KR4.  CutA1 can be found in bacteria, plants, animals and humans [Ref] . The protein was originally identified in a gene locus cutA of Escherichia coli  [Ref] .  Several of CutA1 homologue have been crystallized previously (1VHF, E.Coli; 2E66, Pyrococcus Horikoshii).  In these structures CutA1 protein is a trimer.  Molecular genetics studies on the E. coli cutA locus showed that some mutations lead to copper sensitivity due to its increased uptake [Ref] .  CutA1 may be involved in the tuning of a disulphide bond cascade in bacteria and mammals, acting as the PII proteins do in the nitrogen signal cascade in bacteria and plants.

    Ligand Summary





    1. (No Results)


      Discuss this publication
    2. (No Results)


      Discuss this publication
    3. (No Results)


      Discuss this publication
    Tag page

    Files (0)

    You must login to post a comment.
    All content on this site is licensed under a Creative Commons Attribution 3.0 License
    Powered by MindTouch