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1vpv

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

    Title Crystal structure of UPF0230 protein TM1468 (TM1468) from Thermotoga maritima at 2.45 A resolution. To be published
    Site JCSG
    PDB Id 1vpv Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1291,TM1468, 429685
    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 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.42 Rfactor 0.17987
    Waters
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    Solvent Content 48.83

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1vpv
    1. Expansion of the protein repertoire in newly explored environments: human gut microbiome specific protein families
    K Ellrott, L Jaroszewski, W Li, JC Wooley - PLoS computational , 2010 - dx.plos.org
     
    2. Structure of a fatty acid-binding protein from Bacillus subtilis determined by sulfur-SAD phasing using in-house chromium radiation
    J Nan, Y Zhou, C Yang, E Brostromer - Section D: Biological , 2009 - scripts.iucr.org
     

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    Protein Summary

    The gene TM1468 from Thermotoga maritima encodes a putative fatty-acid binding domain protein (NP_229268), from a well-conserved among bacteria DegV family PF02645 COG1307. STRING genome context analysis provides a reliable hit (score 0.98) based on neighbourhood, gene fusion, and co-ocurrence with the uncharacterized protein TM1772. 

    SCOP classifies 1vpv in the alpha/beta class, DAK1/DegV-like superfamily, DegV-like family. DALI top hits are with the DegV family proteins

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    (Z=35),
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    (Z=33), the APC36103 protein
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    (Z=32) and the SPY1493 protien
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    (Z=32). Weaker hits are observed with the dihydroxyacetone kinases
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    and
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    (Z=16).

    The structure of TM1468 protein had been previously solved in a different crystal form and resolution (1MGP). Both solved structures of the TM1468 protein contain co-crystallized palmitic acid, which is consistent with its putative fatty-acid binding function. The TM1468 structure is in a closed conformation, which is probably induced by palmitate binding.

    The fold type of the TM1468 is similar to that of lipoate-protein ligase A from E.coli 1X2G (SufE/NifU fold.)  Lipoate-protein ligase A (LplA) catalyzes the formation of lipoyl-AMP from lipoate and ATP and then transfers the lipoyl moiety to a specific lysine residue on the acyltransferase subunit of α-ketoacid dehydrogenase complexes and on H-protein of the glycine cleavage system.  

    Ligand Summary



    References

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