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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
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1222,TM0655, 90078, 289567
    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 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.06 Rfactor
    Waters
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    Solvent Content 40.40

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    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
     

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    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

    Reviews

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