1gl7: Difference between revisions
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<StructureSection load='1gl7' size='340' side='right'caption='[[1gl7]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1gl7' size='340' side='right'caption='[[1gl7]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gl7]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1gl7]] is a 6 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GL7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl7 OCA], [https://pdbe.org/1gl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gl7 RCSB], [https://www.ebi.ac.uk/pdbsum/1gl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gl7 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl7 OCA], [https://pdbe.org/1gl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gl7 RCSB], [https://www.ebi.ac.uk/pdbsum/1gl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gl7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q04230_ECOLX Q04230_ECOLX] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Coll | [[Category: Coll M]] | ||
[[Category: | [[Category: De La cruz F]] | ||
[[Category: Gomis-Ruth FX]] | |||
[[Category: Moncalian G]] | |||
[[Category: | |||
[[Category: | |||
Latest revision as of 14:59, 13 December 2023
Plasmid coupling protein TrwB in complex with the non-hydrolisable ATP-analogue ADPNP.Plasmid coupling protein TrwB in complex with the non-hydrolisable ATP-analogue ADPNP.
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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