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The Open Protein Structure Annotation Network
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1vr7

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

    Title Crystal structure of S-adenosylmethionine decarboxylase proenzyme (TM0655) from Thermotoga Maritima at 1.2 A resolution. To be Published
    Site JCSG
    PDB Id 1vr7 Target Id 282527
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1222,TM0655, 289567, 90078 Molecular Weight 14784.00 Da.
    Residues 130 Isoelectric Point 5.56
    Sequence mkslgrhlvaefyecdrevldnvqlieqemkqaayesgativtstfhrflpygvsgvvviseshltiht wpeygyaaidlftcgedvdpwkafehlkkalkakrvhvvehergrydeigipedsphkaav
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.20 Rfree 0.15
    Matthews' coefficent 2.06 Rfactor
    Waters 153 Solvent Content 40.40

    Pathway

    Reactions found in Metabolic Reconstruction for TM0655

    Name: adenosylmethionine decarboxylase
    Metabolic Subsystem: Methionine Metabolism
    Reaction: : amet + h --> ametam + co2
    Classification: EC:4.1.1.50
     

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1vr7
    1. Autoindexing with outlier rejection and identification of superimposed lattices
    NK Sauter, BK Poon - Journal of Applied Crystallography, 2010 - scripts.iucr.org
     
    2. Crenarchaeal arginine decarboxylase evolved from an S-adenosylmethionine decarboxylase enzyme
    TN Giles, DE Graham - Journal of Biological Chemistry, 2008 - ASBMB
     
    3. Structure of LP2179, the first representative of Pfam family PF08866, suggests a new fold with a role in amino-acid metabolism
    C Bakolitsa, A Kumar, D Carlton, MD Miller - Section F: Structural , 2009 - scripts.iucr.org
     

    Protein Summary

    The TM0655 gene of Thermotoga maritima encodes an S-adenosylmethionine decarboxylase (AdoMetDC) (EC 4.1.1.50). AdoMetDC is a pyruvoyl-dependent amino acid decarboxylase involved in methionine metabolism and the polyamine biosynthetic pathway. The TM0655 structure reveals the relationship between the prokaryotic and eukaryotic versions of the enzyme (1) with the former presenting a dimeric fold very similar to the eukaryotic AdoMetDC protomer, suggesting an evolutionary link (1) . There is no detectable sequence similarity between the AdoMetDC found in eukaryotes and prokaryotes, except at the site of pyruvoyl group formation, where the key active site residues involved in substrate binding, catalysis and proenzyme processing are structurally conserved (1).


    Ligand Summary



    References

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