2HDF
Crystal structure of the Colicin I receptor Cir from E.coli
Summary for 2HDF
| Entry DOI | 10.2210/pdb2hdf/pdb |
| Related | 2HDI |
| Descriptor | Colicin I receptor, STRONTIUM ION, N-OCTYL-2-HYDROXYETHYL SULFOXIDE, ... (4 entities in total) |
| Functional Keywords | outer membrane, iron transport, tonb box, signal transduction, colicin i receptor, membrane protein, protein transport |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane: P17315 |
| Total number of polymer chains | 1 |
| Total formula weight | 72263.51 |
| Authors | Buchanan, S.K.,Esser, L.,Lukacik, P. (deposition date: 2006-06-20, release date: 2007-05-08, Last modification date: 2024-11-06) |
| Primary citation | Buchanan, S.K.,Lukacik, P.,Grizot, S.,Ghirlando, R.,Ali, M.M.,Barnard, T.J.,Jakes, K.S.,Kienker, P.K.,Esser, L. Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import. Embo J., 26:2594-2604, 2007 Cited by PubMed Abstract: Colicin Ia is a 69 kDa protein that kills susceptible Escherichia coli cells by binding to a specific receptor in the outer membrane, colicin I receptor (70 kDa), and subsequently translocating its channel forming domain across the periplasmic space, where it inserts into the inner membrane and forms a voltage-dependent ion channel. We determined crystal structures of colicin I receptor alone and in complex with the receptor binding domain of colicin Ia. The receptor undergoes large and unusual conformational changes upon colicin binding, opening at the cell surface and positioning the receptor binding domain of colicin Ia directly above it. We modelled the interaction with full-length colicin Ia to show that the channel forming domain is initially positioned 150 A above the cell surface. Functional data using full-length colicin Ia show that colicin I receptor is necessary for cell surface binding, and suggest that the receptor participates in translocation of colicin Ia across the outer membrane. PubMed: 17464289DOI: 10.1038/sj.emboj.7601693 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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