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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
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1440,TM0741
    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 6
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.33 Rfactor 0.17051
    Waters
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    Solvent Content 46.81

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    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
     

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    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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