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The Open Protein Structure Annotation Network
PDB Keyword
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1vjx

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References
    Title Crystal structure of putative ferritin-like diiron-carboxylate protein (TM1526) from Thermotoga maritima at 2.30 A resolution. To be published
    Site JCSG
    PDB Id 1vjx Target Id 283383
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1297,TM1526 Molecular Weight 17192.62 Da.
    Residues 145 Isoelectric Point 4.88
    Sequence mkvsdiltvairleeegerfyrelsehfngeikktfleladqerihaeifrkmsdqenwdevdsylagy afyevfpdtseilrrkdltlkevldiaisvekdsiilyyelkdglvnsdaqktvkkiidqekehlrkll emkrest
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.30 Rfree 0.25652
    Matthews' coefficent 2.80 Rfactor 0.21727
    Waters 60 Solvent Content 55.78

    Ligand Information
    Ligands
    Metals

    Jmol

     

    Protein Summary

    The gene TM1526 from Thermotoga maritima encodes the NP_229326 protein, that belongs to the rubrerythrin group (PF02915) and folds into a ferritin-like AB domain found in Archaea and Bacteria COG1528.  Genome context analysis provides a weak hit (score 0.57) with TM1526 neighbors, the endoglucanases celA (TM1524) and celB (TM1525).

     

    SCOP classifies 1vjx inside the all alpha class, ferritin-like (super)family. A Dali structural similarity search with 1vjx as query yields  as top hits: 2fzf (Z-scr=17) and the bacterioferritin 1nfv (Z-scr=16). 

    The protein is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. These proteins were sequenced from mostly anaerobic or microaerophilic metal-metabolizing and/or nitrogen-fixing microbes.  The proteins containing this domain have broad functions. A subfamily of these proteins is known as DPS (DNA Protecting protein under Starved conditions) proteins.  Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide.   

    Ligand Summary



    References

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