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1vlv

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

    Title Crystal structure of Ornithine carbamoyltransferase (TM1097) from Thermotoga maritima at 2.25 A resolution. To be published
    Site JCSG
    PDB Id 1vlv Target Id 282963
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1260,TM1097, 89297 Molecular Weight 35359.95 Da.
    Residues 313 Isoelectric Point 5.62
    Sequence msvnlkgrslltlldfspeeirylldiskqvkmenrsklrterfkgmtlamifekrstrtrlafetafa eegghpiflspndihlgakesledtarvlgrmvdaimfrgykqetveklaeysgvpvyngltdefhptq aladlmtieenfgrlkgvkvvfmgdtrnnvatslmiacakmgmnfvacgpeelkprsdvfkrcqeivke tdgsvsftsnleealagadvvytdvwasmgeedkekermallkpyqvnervmemtgksetifmhclpav kgqevtyeviegkqsrvwdeaenrkhtikavmiatll
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.25 Rfree 0.21528
    Matthews' coefficent 2.75 Rfactor 0.18917
    Waters 95 Solvent Content 54.99

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    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1vlv
    1. Contribution of Electrostatic Interactions, Compactness and Quaternary Structure to Protein Thermostability: Lessons from Structural Genomics of Thermotoga
    M Robinson-Rechavi, A Alibs, A Godzik - Journal of molecular biology, 2006 - Elsevier
     
    2. Autoindexing with outlier rejection and identification of superimposed lattices
    NK Sauter, BK Poon - Journal of Applied Crystallography, 2010 - scripts.iucr.org
     
    3. Structure of anabolic ornithine carbamoyltransferase from Campylobacter jejuni at 2.7 A resolution
    IG Shabalin, PJ Porebski, DR Cooper - Section F: Structural , 2012 - scripts.iucr.org
     
    4. New Insight into the Transcarbamylase Family: The Structure of Putrescine Transcarbamylase, a Key Catalyst for Fermentative Utilization of Agmatine
    LM Polo, F Gil-Ortiz, A Cantn, V Rubio - PloS one, 2012 - dx.plos.org
     

    Protein Summary


    The gene TM1097 from Thermotoga maritima encodes ornithine carbamoyltransferase COG0078.  The enzyme contains two domains with distinct functions.  The N-terminal domain belongs to the carbamoyl-P binding domain superfamily PF02729, while the C-terminal domain belongs to the aspartate/ornithine binding domain superfamily PF00185.  The enzyme catalyzes the conversion of ornithine and carbamoyl phosphate to citrulline. In mammals this enzyme participates in the urea cycle [Ref] and is located in the mitochondrial matrix. In prokaryotes and eukaryotic microorganisms it is involved in the biosynthesis of arginine. In some bacterial species it is also involved in the degradation of arginine [Ref] (the arginine deaminase pathway).

    Ligand Summary



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