Structure of TonB in Complex with FhuA, E. coli Outer Membrane Receptor
2006; American Association for the Advancement of Science; Volume: 312; Issue: 5778 Linguagem: Inglês
10.1126/science.1128057
ISSN1095-9203
AutoresPeter D. Pawelek, Nathalie Croteau, Christopher Ng‐Thow‐Hing, Cezar M. Khursigara, Natalia Moiseeva, Marc Allaire, James W. Coulton,
Tópico(s)Enzyme Structure and Function
ResumoThe 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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