Nucleotide recognition by CopA, a Cu+-transporting P-type ATPase.
EMBO J
; 28(12): 1782-91, 2009 Jun 17.
Article
em En
| MEDLINE
| ID: mdl-19478797
ABSTRACT
Heavy metal pumps constitute a large subgroup in P-type ion-transporting ATPases. One of the outstanding features is that the nucleotide binding N-domain lacks residues critical for ATP binding in other well-studied P-type ATPases. Instead, they possess an HP-motif and a Gly-rich sequence in the N-domain, and their mutations impair ATP binding. Here, we describe 1.85 A resolution crystal structures of the P- and N-domains of CopA, an archaeal Cu(+)-transporting ATPase, with bound nucleotides. These crystal structures show that CopA recognises the adenine ring completely differently from other P-type ATPases. The crystal structure of the His462Gln mutant, in the HP-motif, a disease-causing mutation in human Cu(+)-ATPases, shows that the Gln side chain mimics the imidazole ring, but only partially, explaining the reduction in ATPase activity. These crystal structures lead us to propose a role of the His and a mechanism for removing Mg(2+) from ATP before phosphoryl transfer.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Trifosfato de Adenosina
/
Adenosina Trifosfatases
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Archaeoglobus fulgidus
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Proteínas Arqueais
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Proteínas de Transporte de Cátions
Idioma:
En
Ano de publicação:
2009
Tipo de documento:
Article