2GRX
Crystal structure of TonB in complex with FhuA, E. coli outer membrane receptor for ferrichrome
Summary for 2GRX
| Entry DOI | 10.2210/pdb2grx/pdb |
| Descriptor | Ferrichrome-iron receptor, MYRISTIC ACID, Protein tonB, ... (10 entities in total) |
| Functional Keywords | beta barrel, outer membrane, heterocomplex, inter-protein beta sheet, protein-protein, metal transport |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 216872.03 |
| Authors | Pawelek, P.D.,Allaire, M.,Coulton, J.W. (deposition date: 2006-04-25, release date: 2006-06-13, Last modification date: 2024-11-13) |
| Primary citation | Pawelek, P.D.,Croteau, N.,Ng-Thow-Hing, C.,Khursigara, C.M.,Moiseeva, N.,Allaire, M.,Coulton, J.W. Structure of TonB in complex with FhuA, E. coli outer membrane receptor. Science, 312:1399-1402, 2006 Cited by PubMed 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. PubMed: 16741125DOI: 10.1126/science.1128057 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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