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The Open Protein Structure Annotation Network
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2iii

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

    Title Crystal structure of the adenosylmethionine decarboxylase (aq_254) from aquifex aeolicus vf5. To be Published
    Site RSGI
    PDB Id 2iii Target Id aae001000254.1
    Molecular Characteristics
    Source Aquifex aeolicus
    Alias Ids TPS12030, Molecular Weight 15199.45 Da.
    Residues 135 Isoelectric Point 5.58
    Sequence maktlglhiladlygvdadkidrvedirellegavkyanltkisshyyqfqphgatgvvllaeshisih twpehglatvdvytcgdpskayramdyiitqlnpkridkqvhergiveeesnqseaeklrsillqv
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.30 Rfree 0.246
    Matthews' coefficent 1.92 Rfactor 0.188
    Waters 89 Solvent Content 36.03

    Ligand Information
    Ligands
    Metals CA (CALCIUM) x 1;MG (MAGNESIUM) x 1

    Jmol

     

    Protein Summary

    The speH gene of Aquifex aelicus 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 structure is identical (backbone RMSD 1.1 Å over 112 residues) to previously determined prokaryotic AdoMetDCs (PDB ids 1tlu, 1vr7) which reveal the relationship between the prokaryotic and eukaryotic versions of the enzyme (1). The prokaryotic AdoMetDC presents 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

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