2grx
From Proteopedia
Crystal structure of TonB in complex with FhuA, E. coli outer membrane receptor for ferrichrome
Structural highlights
FunctionFHUA_ECOLI This receptor binds the ferrichrome-iron ligand. It interacts with the TonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Structure of TonB in complex with FhuA, E. coli outer membrane receptor.,Pawelek PD, Croteau N, Ng-Thow-Hing C, Khursigara CM, Moiseeva N, Allaire M, Coulton JW Science. 2006 Jun 2;312(5778):1399-402. PMID:16741125[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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