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1o5j

    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
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1257,TM1056, 84666
    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 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.05 Rfactor 0.15603
    Waters
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    Solvent Content 39.45

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    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
     

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    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



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