Type III effector NleH2 from Escherichia coli O157:H7 str. Sakai features an atypical protein kinase domain.
Biochemistry
; 53(15): 2433-5, 2014 Apr 22.
Article
em En
| MEDLINE
| ID: mdl-24712300
ABSTRACT
The crystal structure of a C-terminal domain of enterohemorrhagic Escherichia coli type III effector NleH2 has been determined to 2.6 Å resolution. The structure resembles those of protein kinases featuring the catalytic, activation, and glycine-rich loop motifs and ATP-binding site. The position of helix αC and the lack of a conserved arginine within an equivalent HRD motif suggested that the NleH2 kinase domain's active conformation might not require phosphorylation. The activation segment markedly contributed to the dimerization interface of NleH2, which can also accommodate the NleH1-NleH2 heterodimer. The C-terminal PDZ-binding motif of NleH2 provided bases for interaction with host proteins.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Quinases
/
Escherichia coli O157
/
Proteínas de Escherichia coli
Idioma:
En
Revista:
Biochemistry
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
Estados Unidos