1e9s

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|ACTIVITY=
|ACTIVITY=
|GENE= TRWB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= TRWB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9s OCA], [http://www.ebi.ac.uk/pdbsum/1e9s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e9s RCSB]</span>
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[[Category: ring helicase]]
[[Category: ring helicase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:58:13 2008''

Revision as of 16:58, 30 March 2008


PDB ID 1e9s

Drag the structure with the mouse to rotate
, resolution 2.50Å
Sites:
Gene: TRWB (Escherichia coli)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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