1gl7
From Proteopedia
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- | [[Image:1gl7.jpg|left|200px]] | + | [[Image:1gl7.jpg|left|200px]] |
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- | '''PLASMID COUPLING PROTEIN TRWB IN COMPLEX WITH THE NON-HYDROLISABLE ATP-ANALOGUE ADPNP.''' | + | {{Structure |
+ | |PDB= 1gl7 |SIZE=350|CAPTION= <scene name='initialview01'>1gl7</scene>, resolution 3.0Å | ||
+ | |SITE= <scene name='pdbsite=ANA:Anp+Binding+Site+For+Chain+G'>ANA</scene> | ||
+ | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''PLASMID COUPLING PROTEIN TRWB IN COMPLEX WITH THE NON-HYDROLISABLE ATP-ANALOGUE ADPNP.''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1GL7 is a [ | + | 1GL7 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=1GL7 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: type iv secretion system conjugative coupling protein from plasmid]] | [[Category: type iv secretion system conjugative coupling protein from plasmid]] | ||
- | ''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 11:24:36 2008'' |
Revision as of 09:24, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
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. 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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