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dc.contributor.author | Gomis-Rüth, F. Xavier | - |
dc.contributor.author | Moncalián, Gabriel | - |
dc.contributor.author | Pérez-Luque, Rosa | - |
dc.contributor.author | González, Ana | - |
dc.contributor.author | Cabezón, Elena | - |
dc.contributor.author | Cruz, Fernando de la | - |
dc.contributor.author | Coll, Miquel | - |
dc.date.accessioned | 2012-06-19T10:59:22Z | - |
dc.date.available | 2012-06-19T10:59:22Z | - |
dc.date.issued | 2001 | - |
dc.identifier | doi: 10.1038/35054586 | - |
dc.identifier | issn: 0028-0836 | - |
dc.identifier.citation | Nature 409(6820): 637-641 (2001) | - |
dc.identifier.uri | http://hdl.handle.net/10261/51843 | - |
dc.description.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. Transkingdom 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, 20A°, in width, traverses the hexamer. | - |
dc.description.sponsorship | This work was supported by grants from the Ministerio de Educación y Cultura of Spain, the Generalitat de Catlunya and the European Union. | - |
dc.language.iso | eng | - |
dc.publisher | Nature Publishing Group | - |
dc.rights | closedAccess | - |
dc.title | The bacterial conjugation protein TrwB resembles ring helicases and F1-atpase | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1038/35054586 | - |
dc.date.updated | 2012-06-19T10:59:23Z | - |
dc.description.version | Peer Reviewed | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.grantfulltext | none | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | No Fulltext | - |
item.languageiso639-1 | en | - |
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