1QXX
CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF TONB
Summary for 1QXX
| Entry DOI | 10.2210/pdb1qxx/pdb |
| Related | 1IHR |
| Descriptor | TonB protein (2 entities in total) |
| Functional Keywords | tonb dimerization, transport protein |
| Biological source | Escherichia coli |
| Cellular location | Cell inner membrane; Single-pass membrane protein; Periplasmic side: P02929 |
| Total number of polymer chains | 1 |
| Total formula weight | 8563.89 |
| Authors | Koedding, J.,Howard, P.,Kaufmann, L.,Polzer, P.,Lustig, A.,Welte, W. (deposition date: 2003-09-09, release date: 2004-04-06, Last modification date: 2023-08-23) |
| Primary citation | Koedding, J.,Howard, P.,Kaufmann, L.,Polzer, P.,Lustig, A.,Welte, W. Dimerization of TonB is not essential for its binding to the outer membrane siderophore receptor FhuA of Escherichia coli. J.Biol.Chem., 279:9978-9986, 2004 Cited by PubMed Abstract: FhuA belongs to a family of specific siderophore transport systems located in the outer membrane of Escherichia coli. The energy required for the transport process is provided by the proton motive force of the cytoplasmic membrane and is transmitted to FhuA by the protein TonB. Although the structure of full-length TonB is not known, the structure of the last 77 residues of a fragment composed of the 86 C-terminal amino acids was recently solved and shows an intertwined dimer (Chang, C., Mooser, A., Pluckthun, A., and Wlodawer, A. (2001) J. Biol. Chem. 276, 27535-27540). We analyzed the ability of truncated C-terminal TonB fragments of different lengths (77, 86, 96, 106, 116, and 126 amino acid residues, respectively) to bind to the receptor FhuA. Only the shortest TonB fragment, TonB-77, could not effectively interact with FhuA. We have also observed that the fragments TonB-77 and TonB-86 form homodimers in solution, whereas the longer fragments remain monomeric. TonB fragments that bind to FhuA in vitro also inhibit ferrichrome uptake via FhuA in vivo and protect cells against attack by bacteriophage Phi80. PubMed: 14665631DOI: 10.1074/jbc.M311720200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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