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The Open Protein Structure Annotation Network
PDB Keyword
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1rdu

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References
    Title NMR Structure Determination of the Hypothetical Protein TM1290 from Thermotoga Maritima using Automated NOESY Analysis. J.Biomol.NMR 29 403-406 2004
    Site JCSG
    PDB Id 1rdu Target Id 283154
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1276,TM1290 Molecular Weight 12537.39 Da.
    Residues 116 Isoelectric Point 4.86
    Sequence marvaipsvgkdlssmvsdrfaraeyfiiydtesgnvevventiadahgtgpkvvqslvskgveylias nvgrnafetlkaagvkvyrfeggtvqeaidafsegrleelttftreg
      BLAST   FFAS

    Structure Determination
    Method NMR Chains 1

    Ligand Information
    Ligands
    Metals

    Jmol

     

    Protein Summary

    The gene TM1290 from Thermotoga maritima encodes protein belonging to a family of iron-molybdenum cluster-binding proteins that includes NifX, NifB, and NifY, all of which are involved in the synthesis of an iron-molybdenum cofactor (FeMo-co) that binds the active site of the dinitrogenase enzyme (dinitrogenase iron-molybdenum cofactor PF02579). This domain is a predicted small-molecule-binding domain (SMBD) with an alpha/beta fold that is present either as a stand-alone domain (e.g. NifX and NifY) or fused to another conserved domain (e.g. NifB).  NifB appears to be an iron-sulphur source for FeMo-co biosynthesis, while NifX may be associated with the mature FeMo-co, in particular with the addition of homocitrate during the last step of biosynthesis [Ref]. This conserved domain is represented in two of the three major divisions of life (bacteria and archaea).

     

    This is one of several proteins from this family ( 1o13 (T. maritima ortholog TM1816), 2re2, 2kla) solved by JCSG.

    Ligand Summary



    References

    Reviews

    References

     

    1. Rangaraj P, Ruttimann-Johnson C, Shah VK, and Ludden PW Accumulation of 55Fe-labeled precursors of the iron-molybdenum cofactor of nitrogenase on NifH and NifX of Azotobacter vinelandii. J Biol Chem. 2001 May 11; 276(19):15968-74 PubMed HubMed doi:10.1074/jbc.M100907200 pmid:11279153.

       


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