1GKI

Plasmid coupling protein TrwB in complex with ADP and Mg2+.

Summary for 1GKI

• Entry DOI: 10.2210/pdb1gki/pdb
• Related: 1E9R 1E9S 1GL6 1GL7
• Descriptor: CONJUGAL TRANSFER PROTEIN TRWB, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: coupling protein, bacterial conjugation, f1-atpase-like quaternary structure, ring helicases
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 6
• Total formula weight: 295190.16

Authors

Gomis-Ruth, F.X.,Moncalian, G.,De La cruz, F.,Coll, M. (deposition date: 2001-08-14, 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

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

Experimental method

X-RAY DIFFRACTION (3 Å)