2grx | pdb_00002grx
Crystal structure of TonB in complex with FhuA, E. coli outer membrane receptor for ferrichrome
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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 PO4, FTT, DPO, DAO, MYR, EAP and FCI 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
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