1gl7
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The transfer of DNA across membranes and between cells is a central | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Coll, M.]] | [[Category: Coll, M.]] | ||
| - | [[Category: Cruz, F | + | [[Category: Cruz, F De La.]] |
| - | [[Category: Gomis-Ruth, F | + | [[Category: Gomis-Ruth, F X.]] |
[[Category: Moncalian, G.]] | [[Category: Moncalian, G.]] | ||
[[Category: ANP]] | [[Category: ANP]] | ||
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[[Category: type iv secretion system conjugative coupling protein from plasmid]] | [[Category: type iv secretion system conjugative coupling protein from plasmid]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:17 2008'' |
Revision as of 10:51, 21 February 2008
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PLASMID COUPLING PROTEIN TRWB IN COMPLEX WITH THE NON-HYDROLISABLE ATP-ANALOGUE ADPNP.
Overview
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.
About this Structure
1GL7 is a Single protein structure of sequence from Escherichia coli with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase., Gomis-Ruth FX, Moncalian G, Perez-Luque R, Gonzalez A, Cabezon E, de la Cruz F, Coll M, Nature. 2001 Feb 1;409(6820):637-41. PMID:11214325
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