1gl7
From Proteopedia
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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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