Crystallization and data collection of the nucleotide-binding domain of Mg-ATPase.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 65(Pt 3): 223-5, 2009 Mar 01.
Article
em En
| MEDLINE
| ID: mdl-19255470
ABSTRACT
Understanding of how P-type ATPases work would greatly benefit from the elucidation of more high-resolution structures. The nucleotide-binding domain of Mg-ATPase was selected for structural studies because Mg-ATPase is closely related to eukaryotic Ca-ATPase and Na,K-ATPase while the nucleotide-binding domain itself has diverged substantially. Two fragments of Mg-ATPase were cloned in Escherichia coli and purified. The entire cytoplasmic loop (residues 367-673), consisting of the phosphorylation and nucleotide-binding domains, expressed well and was purified in large quantities. The smaller 19.5 kDa nucleotide-binding domain (residues 383-545) expressed less well but formed crystals that diffracted to a resolution of 1.53 A which will be used for molecular replacement.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Membrana Transportadoras
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ATPase de Ca(2/) e Mg(2/)
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Adenosina Trifosfatases
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Proteínas de Escherichia coli
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Escherichia coli
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Nucleotídeos
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2009
Tipo de documento:
Article
País de afiliação:
Dinamarca