2grx
From Proteopedia
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Crystal structure of TonB in complex with FhuA, E. coli outer membrane receptor for ferrichrome
Overview
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.
About this Structure
2GRX is a Protein complex structure of sequences from Escherichia coli with , , , , , and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 17:34:40 2008
Categories: Escherichia coli | Protein complex | Allaire, M. | Coulton, J W. | Pawelek, P D. | DAO | DPO | EAP | FCI | FTT | MYR | PO4 | Beta barrel | Heterocomplex | Inter-protein beta sheet | Outer membrane | Protein-protein
