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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
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    Molecular Characteristics
    Source
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    Alias Ids TPS12030, 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 1.92 Rfactor 0.188
    Waters
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    Solvent Content 36.03

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

    Jmol

     
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    Google Scholar output for 2iii

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    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

    Reviews

    References

     

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