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The Open Protein Structure Annotation Network
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2gvi

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

    Title Crystal structure of (10640422) from THERMOPLASMA ACIDOPHILUM at 1.87 A resolution. To be published
    Site JCSG
    PDB Id 2gvi Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1466,10640422, PF02663, 90577
    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 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.87 Rfactor 0.19
    Waters
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    Solvent Content 56.79

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2gvi
    1. Ligands in crystal structures that aid in functional characterization
    AE Speers, BF Cravatt - Acta Crystallographica Section F: Structural , 2010 - scripts.iucr.org
     
    2. Structures of three members of Pfam PF02663 (FmdE) implicated in microbial methanogenesis reveal a conserved+ core domain and an auxiliary C-terminal treble-
    HL Axelrod, D Das, P Abdubek, T Astakhova - Section F: Structural , 2010 - scripts.iucr.org
     

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    Protein Summary

    The gene Ta1109 from Thermoplasma acidophilum encodes the NP_394568 protein, a putative subunit E of the formylmethanofuran dehydrogenase PF02663 EC:1.2.99.5 COG2191.  

    The 2gvi structure belongs to the class of alpha and beta (a+b) proteins and reveals FmdE/GAPDH domain-like fold SCOP55346, inside the FmdE-like (super)family. The structure of homologous enzyme from Desulfitobacterium hafniense has been solved by Jcsg (

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    , Z=16, see Topsan).  Another structure similar to 2gvi is the tungsten formylmethanofuran dehydrogenase
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    (Z=12).

    The Fmd enzyme  catalyzes the reaction: formylmethanofuran + H2O + acceptor --> CO2 + methanofuran + reduced acceptor.  It requires  2 cofactors: molybdenum or tungsten, and pterin.  This enzyme participates in folate biosynthesis.  

    Ligand Summary



    References

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