2I88
Crystal structure of the Channel-forming Domain of Colicin E1
Summary for 2I88
| Entry DOI | 10.2210/pdb2i88/pdb |
| Related | 1A87 1CII 1COL 1ujw |
| Descriptor | Colicin-E1 (2 entities in total) |
| Functional Keywords | protein-membrane interactions, toxin-membrane interactions, toxin structure, voltage-gated channel, colicin, membrane protein |
| Biological source | Escherichia coli |
| Cellular location | Cell membrane ; Multi-pass membrane protein : P02978 |
| Total number of polymer chains | 1 |
| Total formula weight | 21196.42 |
| Authors | Elkins, P.,Bunker, A.,Cramer, W.A.,Stauffacher, C.V. (deposition date: 2006-09-01, release date: 2006-09-26, Last modification date: 2024-02-21) |
| Primary citation | Elkins, P.,Bunker, A.,Cramer, W.A.,Stauffacher, C.V. A mechanism for toxin insertion into membranes is suggested by the crystal structure of the channel-forming domain of colicin E1 Structure, 5:443-458, 1997 Cited by PubMed Abstract: Channel-forming colicins, including colicin E1, are a sub-family of bacteriocins. The toxic action of colicin E1 is derived from its ability to form a voltage-gated channel, which causes depolarization of the cytoplasmic membrane of sensitive Escherichia coli cells. In this process, the toxin-like colicin E1 molecule must undergo a substantial structural transition from a soluble state, in which it binds the target cell, to a membrane-bound state. Details of the structural changes that accompany this conversion may be directly applicable to other channel-forming toxins, as well as to the mechanism by which proteins insert into or cross membranes. PubMed: 9083117DOI: 10.1016/S0969-2126(97)00200-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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