The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase

F. Xavier Gomis-Rüth, Gabriel Moncalián, Rosa Pérez-Luque, Ana González, Elena Cabezón, Fernando de la Cruz and Miquel Coll ()
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F. Xavier Gomis-Rüth: Institut de Biologia Molecular de Barcelona, CSIC
Gabriel Moncalián: Universidad de Cantabria
Rosa Pérez-Luque: Institut de Biologia Molecular de Barcelona, CSIC
Ana González: EMBL Hamburg Outstation, c/o DESY
Elena Cabezón: Universidad de Cantabria
Fernando de la Cruz: Universidad de Cantabria
Miquel Coll: Institut de Biologia Molecular de Barcelona, CSIC

Nature, 2001, vol. 409, issue 6820, 637-641

Abstract: 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 plants1 or fungi2 and even bacterial sporulation3 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 α/β topology, reminiscent of RecA and DNA ring helicases, and an all-α domain. Six equivalent protein monomers associate to form an almost spherical quaternary structure that is strikingly similar to F1-ATPase. A central channel, 20 Å in width, traverses the hexamer.

Date: 2001
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DOI: 10.1038/35054586

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