Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E. coli and enteropathogenic Y. pseudotuberculosis.
Structure
; 20(7): 1233-43, 2012 Jul 03.
Article
em En
| MEDLINE
| ID: mdl-22658748
ABSTRACT
Intimins and invasins are virulence factors produced by pathogenic Gram-negative bacteria. They contain C-terminal extracellular passenger domains that are involved in adhesion to host cells and N-terminal ß domains that are embedded in the outer membrane. Here, we identify the domain boundaries of an E. coli intimin ß domain and use this information to solve its structure and the ß domain structure of a Y. pseudotuberculosis invasin. Both ß domain structures crystallized as monomers and reveal that the previous range of residues assigned to the ß domain also includes a protease-resistant domain that is part of the passenger. Additionally, we identify 146 nonredundant representative members of the intimin/invasin family based on the boundaries of the highly conserved intimin and invasin ß domains. We then use this set of sequences along with our structural data to find and map the evolutionarily constrained residues within the ß domain.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas Recombinantes de Fusão
/
Yersinia pseudotuberculosis
/
Adesinas Bacterianas
/
Proteínas de Escherichia coli
/
Escherichia coli Êntero-Hemorrágica
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Structure
Assunto da revista:
BIOLOGIA MOLECULAR
/
BIOQUIMICA
/
BIOTECNOLOGIA
Ano de publicação:
2012
Tipo de documento:
Article
País de afiliação:
Estados Unidos