1GL7
Plasmid coupling protein TrwB in complex with the non-hydrolisable ATP-analogue ADPNP.
Summary for 1GL7
| Entry DOI | 10.2210/pdb1gl7/pdb |
| Related | 1E9R 1E9S 1GKI 1GL6 |
| Descriptor | CONJUGAL TRANSFER PROTEIN TRWB, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | coupling protein, type iv secretion system conjugative coupling protein from plasmid |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 6 |
| Total formula weight | 295101.44 |
| Authors | Gomis-Ruth, F.X.,Moncalian, G.,De La cruz, F.,Coll, M. (deposition date: 2001-08-28, release date: 2002-05-16, Last modification date: 2023-12-13) |
| Primary citation | Gomis-Ruth, F.X.,Moncalian, G.,Perez-Luque, R.,Gonzalez, A.,Cabezon, E.,De La Cruz, F.,Coll, M. The Bacterial Conjugation Protein Trwb Resembles Ring Helicases and F1-ATPase Nature, 409:637-, 2001 Cited by PubMed Abstract: The transfer of DNA across membranes and between cells is a central biological process; however, its molecular mechanism remains unknown. In prokaryotes, trans-membrane passage by bacterial conjugation, is the main route for horizontal gene transfer. It is the means for rapid acquisition of new genetic information, including antibiotic resistance by pathogens. Trans-kingdom gene transfer from bacteria to plants or fungi and even bacterial sporulation are special cases of conjugation. An integral membrane DNA-binding protein, called TrwB in the Escherichia coli R388 conjugative system, is essential for the conjugation process. This large multimeric protein is responsible for recruiting the relaxosome DNA-protein complex, and participates in the transfer of a single DNA strand during cell mating. Here we report the three-dimensional structure of a soluble variant of TrwB. The molecule consists of two domains: a nucleotide-binding domain of alpha/beta topology, reminiscent of RecA and DNA ring helicases, and an all-alpha domain. Six equivalent protein monomers associate to form an almost spherical quaternary structure that is strikingly similar to F1-ATPase. A central channel, 20 A in width, traverses the hexamer. PubMed: 11214325DOI: 10.1038/35054586 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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