1gl6
From Proteopedia
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| - | [[Image:1gl6.jpg|left|200px]]<br /><applet load="1gl6" size=" | + | [[Image:1gl6.jpg|left|200px]]<br /><applet load="1gl6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gl6, resolution 2.8Å" /> | caption="1gl6, resolution 2.8Å" /> | ||
'''PLASMID COUPLING PROTEIN TRWB IN COMPLEX WITH THE NON-HYDROLYSABLE GTP ANALOGUE GDPNP'''<br /> | '''PLASMID COUPLING PROTEIN TRWB IN COMPLEX WITH THE NON-HYDROLYSABLE GTP ANALOGUE GDPNP'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GL6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CL, GNP and EPE as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=GNA:Gnp Binding Site For Chain F'>GNA</scene>. Full crystallographic information is available from [http:// | + | 1GL6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=GNP:'>GNP</scene> and <scene name='pdbligand=EPE:'>EPE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=GNA:Gnp+Binding+Site+For+Chain+F'>GNA</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: type iv secretion system]] | [[Category: type iv secretion system]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:40:50 2008'' |
Revision as of 07:40, 3 February 2008
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PLASMID COUPLING PROTEIN TRWB IN COMPLEX WITH THE NON-HYDROLYSABLE GTP ANALOGUE GDPNP
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
1GL6 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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