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The Open Protein Structure Annotation Network
PDB Keyword
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2anu

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

    Title Crystal structure of Predicted metal-dependent phosphoesterase (PHP family) (tm0559) from THERMOTOGA MARITIMA at 2.40 A resolution. To be published
    Site JCSG
    PDB Id 2anu Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1214,TM0559, 84920
    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 2.92 Rfactor 0.169
    Waters
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    Solvent Content 57.54

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2anu
    1. Formation of tight junction: determinants of homophilic interaction between classic claudins
    J Piontek, L Winkler, H Wolburg, SL Mller, N Zuleger - The FASEB Journal, 2008 - FASEB
     
    2. The Structure of T. aquaticus DNA Polymerase III Is Distinct from Eukaryotic Replicative DNA Polymerases
    S Bailey, RA Wing, TA Steitz - Cell, 2006 - Elsevier
     
    3. Research Non-homologous isofunctional enzymes: A systematic analysis of alternative solutions in enzyme evolution
    MV Omelchenko, MY Galperin, YI Wolf, EV Koonin - 2010 - biomedcentral.com
     
    4. Crystal structure of monofunctional histidinol phosphate phosphatase from Thermus thermophilus HB8
    R Omi, M Goto, I Miyahara, M Manzoku, A Ebihara - Biochemistry, 2007 - ACS Publications
     
    5. Crystal structure of a metal_dependent phosphoesterase (YP_910028. 1) from Bifidobacterium adolescentis: Computational prediction and experimental validation of
    GW Han, J Ko, CL Farr, MC Deller, Q Xu - Proteins: Structure, , 2011 - Wiley Online Library
     

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    Protein Summary


    The TM0559 gene from Thermotoga maritima encodes a putative meta-dependent phosphoesterase domain, a member of the PHP (Polymerase and Histidinol Phosphatase EC:3.1.3.15) superfamily PF02811 COG0613.  The PHP phosphatase domain is contained within the alpha subunits of bacterial DNA polymerase III and two distinct family X DNA polymerases [Ref].  The conserved motifs required for phospho-esterase activity are intact in the archaeal DNA polymerase subunits, but are disrupted in their eukaryotic orthologs. A hypothesis is proposed that bacterial and archaeal replicative DNA polymerases possess intrinsic phosphatase activity that hydrolyzes the pyrophosphate released during nucleotide polymerization.  The pyrophosphate hydrolysis may be necessary to drive the polymerization reaction forward.

     
     
     
     

     

     
     
     

    Ligand Summary



    References

    Reviews

    References

     

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