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The Open Protein Structure Annotation Network
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1vlh

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

    Title Crystal structure of Phosphopantetheine adenylyltransferase (TM0741) from Thermotoga maritima at 2.20 A resolution. To be published
    Site JCSG
    PDB Id 1vlh Target Id 359843
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1440,TM0741 Molecular Weight 18248.39 Da.
    Residues 161 Isoelectric Point 6.44
    Sequence mkavypgsfdpitlghvdiikralsifdelvvlvtenprkkcmftleerkklieevlsdldgvkvdvhh gllvdylkkhgikvlvrglravtdyeyelqmalankklysdletvfliasekfsfissslvkevalygg dvtewvppevaralneklkegkr
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 6
    Resolution (Å) 2.20 Rfree 0.22687
    Matthews' coefficent 2.33 Rfactor 0.17051
    Waters 258 Solvent Content 46.81

    Pathway

    Reactions found in Metabolic Reconstruction for TM0741

    Name: pantetheine-phosphate adenylyltransferase
    Metabolic Subsystem: Pantothenate and CoA Metabolism
    Reaction: : atp + h + pan4p <==> dpcoa + ppi
    Classification: EC:2.7.7.3
     

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1vlh
    1. 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
     
    2. Crystal structure of phosphopantetheine adenylyltransferase from Enterococcus faecalis in the ligand-unbound state and in complex with ATP and pantetheine
    HJ Yoon, JY Kang, B Mikami, HH Lee, SW Suh - Molecules and cells, 2011 - Springer
     
    3. Structures of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei
    TE Edwards, DJ Leibly, J Bhandari - Section F: Structural , 2011 - scripts.iucr.org
     

    Protein Summary

    The gene TM0741 from Thermotoga maritima encodes the enzyme phosphopantetheine adenylyltransferase (PPAT) COG0669, a/b protein SCOP.  The enzyme belongs to a transferases superfamily.  The alternative names are antetheine-phosphate adenylyltransferase and dephospho-CoA pyrophosphorylase.  PPAT is an essential enzyme in bacteria that catalyses the rate-limiting step in coenzyme A (CoA) biosynthesis, by transferring an adenylyl group from ATP to 4'-phosphopantetheine to yield dephospho-CoA (dPCoA).  Because bacterial PPAT and mammalian PPAT are dissimilar, this class of enzymes is an attractive antibacterial target.  Several high resolution structures of the enzyme homologues from other bacterial species have been solved: 1OD6Thermus thermophilus; 3F3M, Staphylococcus aureus; 1O6BBacillus subtilis.

    Ligand Summary



    References

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