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The Open Protein Structure Annotation Network
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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 283326
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1291,TM1468, 429685 Molecular Weight 32572.90 Da.
    Residues 288 Isoelectric Point 5.86
    Sequence mkvkilvdstadvpfswmekydidsiplyvvwedgrsepderepeeimnfykrireagsvpktsqpsve dfkkrylkykeedydvvlvltlssklsgtynsavlaskevdipvyvvdtllasgaiplparvaremlen gatieevlkkldermknkdfkaifyvsnfdylvkggrvskfqgfvgnllkirvclhiengelipyrkvr gdkkaiealieklredtpegsklrvigvhadneagvvellntlrksyevvdeiispmgkvitthvgpgt vgfgievlerkr
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.45 Rfree 0.25188
    Matthews' coefficent 2.42 Rfactor 0.17987
    Waters 107 Solvent Content 48.83

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    Ligand Information
    Ligands
    Metals

    Jmol

     
    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
     

    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 PDB:2dt8 (Z=35), PDB:3fys (Z=33), the APC36103 protein PDB:1pzx (Z=32) and the SPY1493 protien PDB:2g7z (Z=32). Weaker hits are observed with the dihydroxyacetone kinases PDB:3ct4 and PDB:2iu4 (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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