PMID:11428898
| Citation |
Schrag, JD, Huang, W, Sivaraman, J, Smith, C, Plamondon, J, Larocque, R, Matte, A and Cygler, M (2001) The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway. J. Mol. Biol. 310:419-31 |
|---|---|
| Abstract |
MoeA is involved in synthesis of the molybdopterin cofactor, although its function is not yet clearly defined. The three-dimensional structure of the Escherichia coli protein was solved at 2.2 A resolution. The locations of highly conserved residues among the prokaryotic and eukaryotic MoeA homologs identifies a cleft in the dimer interface as the likely functional site. Of the four domains of MoeA, domain 2 displays a novel fold and domains 1 and 4 each have only one known structural homolog. Domain 3, in contrast, is structurally similar to many other proteins. The protein that resembles domain 3 most closely is MogA, another protein required for molybdopterin cofactor synthesis. The overall similarity between MoeA and MogA, and the similarities in a constellation of residues that are strongly conserved in MoeA, suggests that these proteins bind similar ligands or substrates and may have similar functions. |
| Links |
PubMed Online version:10.1006/jmbi.2001.4771 |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Coenzymes/biosynthesis; Coenzymes/chemistry; Coenzymes/metabolism; Conserved Sequence; Crystallography, X-Ray; Dimerization; Escherichia coli/enzymology; Escherichia coli Proteins; Light; Metalloproteins/biosynthesis; Metalloproteins/chemistry; Metalloproteins/metabolism; Models, Molecular; Molecular Sequence Data; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Pteridines/chemistry; Pteridines/metabolism; Scattering, Radiation; Sequence Alignment; Sulfurtransferases/chemistry; Sulfurtransferases/metabolism |
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