Structure of TonB in complex with FhuA, E. coli outer membrane receptor.
Science
; 312(5778): 1399-402, 2006 Jun 02.
Article
em En
| MEDLINE
| ID: mdl-16741125
ABSTRACT
The cytoplasmic membrane protein TonB spans the periplasm of the Gram-negative bacterial cell envelope, contacts cognate outer membrane receptors, and facilitates siderophore transport. The outer membrane receptor FhuA from Escherichia coli mediates TonB-dependent import of ferrichrome. We report the 3.3 angstrom resolution crystal structure of the TonB carboxyl-terminal domain in complex with FhuA. TonB contacts stabilize FhuA's amino-terminal residues, including those of the consensus Ton box sequence that form an interprotein beta sheet with TonB through strand exchange. The highly conserved TonB residue arginine-166 is oriented to form multiple contacts with the FhuA cork, the globular domain enclosed by the beta barrel.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas da Membrana Bacteriana Externa
/
Proteínas de Escherichia coli
/
Escherichia coli
/
Proteínas de Membrana
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article