The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Crystal structure of Homoserine O-succinyltransferase (EC (Homoserine O-transsuccinylase) (HTS) (tm0881) from THERMOTOGA MARITIMA at 2.52 A resolution. To be published
    Site JCSG
    PDB Id 2h2w Target Id 359866
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1441,TM0881, 60680117, PF04204 Molecular Weight 35262.81 Da.
    Residues 300 Isoelectric Point 6.27
    Sequence mpinvpsglpavkvlakegifvmtekraihqdirpleililnlmpdkikteiqllrllgntplqvnvtl lytethkpkhtpiehilkfyttfsavkdrkfdgfiitgapvellpfeevdyweelteimewsrhnvyst mficwaaqaglyyfygipkyelpqklsgvykhrvakdsvlfrghddffwaphsrytevkkedidkvpel eilaesdeagvyvvankserqifvtghpeydrytlrdeyyrdigrnlkvpipanyfpnddptktpiltw wshahlffsnwlnyciyqktpyrl
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.52 Rfree 0.274
    Matthews' coefficent 2.88 Rfactor 0.19
    Waters 16 Solvent Content 56.96

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    Ligand Information


    Google Scholar output for 2h2w
    1. Toward better refinement of comparative models: predicting loops in inexact environments
    BD Sellers, K Zhu, S Zhao, RA Friesner - Proteins: Structure, , 2008 - Wiley Online Library
    2. Amino acid biosynthesis: new architectures in allosteric enzymes
    G Curien, V Biou, C Mas-Droux - Plant Physiology and , 2008 - Elsevier
    3. Domain definition and target classification for CASP7
    ND Clarke, I Ezkurdia, J Kopp, RJ Read - Proteins: Structure, , 2007 - Wiley Online Library
    4. Identification of catalytic cysteine, histidine, and lysine residues in Escherichia coli homoserine transsuccinylase
    K Ziegler, SM Noble, E Mutumanje, B Bishop - Biochemistry, 2007 - ACS Publications
    5. Assessing the roles of essential functional groups in the mechanism of homoserine succinyltransferase
    DM Coe, RE Viola - Archives of biochemistry and biophysics, 2007 - Elsevier

    Protein Summary

    [Information obtained from Refinement summary by Chloe Zubieta]

    TM0881 is a homoserine O-succinyltransferase (HTS) with a typical Rossmann fold topology.The structure was solved by molecular replacement using as a search model the previously determined structure of the Bacillus cereus enzyme (PDB accession code 2GHR).Unlike 2GHR the dimerization interface for TM0881 does not involve strand exchange.
    Based on previous biochemical studies delineating putative active site residues including Cys142, and comparison with the structurally related HTS from B. cereus, the active site of T. maritima HTS  is most likely defined by the highly conserved catalytic triad consisting of Cys142, His234, and Glu236.

    Conserved domain searches with the primary amino acid sequence of TM0881 identify a glutamine amidotransferase domain (GATase-1).These searches, however, do not identify the Cys-His-Glu catalytic triad. Also, it must be noted that the catalytic triad of GATase-1 type enzymes is NOT conserved within HTSs.The structural characterization of this enzyme reinforces the location of a catalytic triad first identified in B. cereus HTS.Comparisons with annotated HTSs show an extremely highly conserved Cys-His-Glu catalytic triad.


    Ligand Summary





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