1e9r: Difference between revisions
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[[Image:1e9r.jpg|left|200px]] | [[Image:1e9r.jpg|left|200px]] | ||
'''BACTERIAL CONJUGATIVE COUPLING PROTEIN TRWBDELTAN70. TRIGONAL FORM IN COMPLEX WITH SULPHATE.''' | {{Structure | ||
|PDB= 1e9r |SIZE=350|CAPTION= <scene name='initialview01'>1e9r</scene>, resolution 2.40Å | |||
|SITE= <scene name='pdbsite=SO1:So4+Binding+Site+For+Residue+G602+Nucleotide-Binding+Sit+...'>SO1</scene> | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= TRWB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''BACTERIAL CONJUGATIVE COUPLING PROTEIN TRWBDELTAN70. TRIGONAL FORM IN COMPLEX WITH SULPHATE.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E9R is a [ | 1E9R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9R OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11214325 11214325] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: coupling protein]] | [[Category: coupling protein]] | ||
[[Category: f1-atpase-like quaternary structure]] | [[Category: f1-atpase-like quaternary structure]] | ||
[[Category: ring | [[Category: ring helicase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:52:13 2008'' | ||
Revision as of 11:52, 20 March 2008
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| , resolution 2.40Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Gene: | TRWB (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BACTERIAL CONJUGATIVE COUPLING PROTEIN TRWBDELTAN70. TRIGONAL FORM IN COMPLEX WITH SULPHATE.
OverviewOverview
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 StructureAbout this Structure
1E9R is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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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