1E9R
Bacterial conjugative coupling protein TrwBdeltaN70. Trigonal form in complex with sulphate.
1E9R の概要
| エントリーDOI | 10.2210/pdb1e9r/pdb |
| 関連するPDBエントリー | 1E9S |
| 分子名称 | CONJUGAL TRANSFER PROTEIN TRWB, SULFATE ION (3 entities in total) |
| 機能のキーワード | coupling protein, bacterial conjugation, f1-atpase-like quaternary structure, ring helicases |
| 由来する生物種 | ESCHERICHIA COLI |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 293469.76 |
| 構造登録者 | Gomis-Rueth, F.X.,Moncalian, G.,Cabezon, E.,de la Cruz, F.,Coll, M. (登録日: 2000-10-26, 公開日: 2001-02-06, 最終更新日: 2024-05-08) |
| 主引用文献 | Gomis-Rueth, 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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