1e9s
From Proteopedia
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| - | [[Image:1e9s.gif|left|200px]]<br /> | + | [[Image:1e9s.gif|left|200px]]<br /><applet load="1e9s" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1e9s" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1e9s, resolution 2.50Å" /> | caption="1e9s, resolution 2.50Å" /> | ||
'''BACTERIAL CONJUGATIVE COUPLING PROTEIN TRWBDELTAN70. UNBOUND MONOCLINIC FORM.'''<br /> | '''BACTERIAL CONJUGATIVE COUPLING PROTEIN TRWBDELTAN70. UNBOUND MONOCLINIC FORM.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E9S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. | + | 1E9S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Known structural/functional Site: <scene name='pdbsite=NBS:Nucleotide-Binding Site Around Lys136 Of Each Chain'>NBS</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E9S OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ring helicases]] | [[Category: ring helicases]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:07:07 2007'' |
Revision as of 12:57, 18 December 2007
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BACTERIAL CONJUGATIVE COUPLING PROTEIN TRWBDELTAN70. UNBOUND MONOCLINIC FORM.
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
1E9S is a Single protein structure of sequence from Escherichia coli. 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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