The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway.
J Mol Biol
; 310(2): 419-31, 2001 Jul 06.
Article
en En
| MEDLINE
| ID: mdl-11428898
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.
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Banco de datos:
MEDLINE
Asunto principal:
Sulfurtransferasas
/
Coenzimas
/
Proteínas de Escherichia coli
/
Escherichia coli
/
Metaloproteínas
Idioma:
En
Año:
2001
Tipo del documento:
Article