1GL7

Plasmid coupling protein TrwB in complex with the non-hydrolisable ATP-analogue ADPNP.

1GL7 の概要

• エントリーDOI: 10.2210/pdb1gl7/pdb
• 関連するPDBエントリー: 1E9R 1E9S 1GKI 1GL6
• 分子名称: CONJUGAL TRANSFER PROTEIN TRWB, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: coupling protein, type iv secretion system conjugative coupling protein from plasmid
• 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: 295101.44

構造登録者

Gomis-Ruth, F.X.,Moncalian, G.,De La cruz, F.,Coll, M. (登録日: 2001-08-28, 公開日: 2002-05-16, 最終更新日: 2023-12-13)

主引用文献

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

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: 11214325
DOI: 10.1038/35054586

実験手法

X-RAY DIFFRACTION (3 Å)