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1vra

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

    Title Crystal structure of Arginine biosynthesis bifunctional protein argJ (10175521) from Bacillus halodurans at 2.00 A resolution. To be published
    Site JCSG
    PDB Id 1vra Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1367,10175521, RER070207001253, 289331, 289435
    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 3.05 Rfactor 0.13967
    Waters
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    Solvent Content 59.62

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1vra
    1. PIEEfficient filters and coarse grained potentials for unbound proteinprotein docking
    DVS Ravikant, R Elber - Proteins: Structure, Function, and , 2010 - Wiley Online Library
     
    2. The molecular structure of ornithine acetyltransferase from Mycobacterium tuberculosis bound to ornithine, a competitive inhibitor
    R Sankaranarayanan, MM Cherney, C Garen - Journal of molecular , 2010 - Elsevier
     
    3. Coulomb energies of protein-protein complexes with monopole-free charge distributions
    M Das, G Basu - Journal of Molecular Graphics and Modelling, 2009 - Elsevier
     
    4. Preliminary X-ray crystallographic analysis of ornithine acetyltransferase (Rv1653) from Mycobacterium tuberculosis
    R Sankaranarayanan, CR Garen - Section F: Structural , 2009 - scripts.iucr.org
     
    5. SYSTEM AND USES FOR GENERATING DATABASES OF PROTEIN SECONDARY STRUCTURES INVOLVED IN INTER-CHAIN PROTEIN INTERACTIONS
    AL Jochim, PS Arora - US Patent App. 12/753,638, 2010 - Google Patents
     

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    Protein Summary


    The gene 10175521 from Bacillus halodurans encodes  the enzyme form ornithine acetyltransferase (OAT) family, also referred to as ArgJ PF01960.  OAT is the bifunctional enzyme and catalyzes the first and fifth steps in arginine biosynthesis, coupling acetylation of glutamate EC.2.3.1.1 with deacetylation of N-acetylornithine EC.2.3.1.35.  The coupling  of glutamate acetylation allows recycling of the acetyl group in the arginine biosynthetic pathway.  Some members of this family are inhibited by L-arginine.  The active enzyme is a heterotetramer of two alpha and two beta chains, where the alpha and beta chains are formed as the result of autocatalytic cleavage.  The enzyme belongs to the class of alpha and beta proteins (a+b) and reveals DmpA/ArgJ-like fold type SCOP.  Several structures of its homologue from STREPTOMYCES CLAVULIGERUS have been solved: 1VZ6, 2W4N, 2V4I.

    Ligand Summary



    References

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