4fhr: Difference between revisions
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[[ | ==Crystal structure of the complex between the flagellar motor proteins FliG and FliM.== | ||
<StructureSection load='4fhr' size='340' side='right' caption='[[4fhr]], [[Resolution|resolution]] 1.93Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4fhr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FHR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FHR FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ajc|3ajc]], [[1lkv|1lkv]], [[3hjl|3hjl]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FliM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]), fliG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fhr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fhr RCSB], [http://www.ebi.ac.uk/pdbsum/4fhr PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The flagellar motor is one type of propulsion device of motile bacteria. The cytoplasmic ring (C-ring) of the motor interacts with the stator to generate torque in clockwise and counterclockwise directions. The C-ring is composed of three proteins, FliM, FliN, and FliG. Together they form the "switch complex" and regulate switching and torque generation. Here we report the crystal structure of the middle domain of FliM in complex with the middle and C-terminal domains of FliG that shows the interaction surface and orientations of the proteins. In the complex, FliG assumes a compact conformation in which the middle and C-terminal domains (FliG(MC)) collapse and stack together similarly to the recently published structure of a mutant of FliG(MC) with a clockwise rotational bias. This intramolecular stacking of the domains is distinct from the intermolecular stacking seen in other structures of FliG. We fit the complex structure into the three-dimensional reconstructions of the motor and propose that the cytoplasmic ring is assembled from 34 FliG and FliM molecules in a 1:1 fashion. | |||
Structure of flagellar motor proteins in complex allows for insights into motor structure and switching.,Vartanian AS, Paz A, Fortgang EA, Abramson J, Dahlquist FW J Biol Chem. 2012 Oct 19;287(43):35779-83. doi: 10.1074/jbc.C112.378380. Epub, 2012 Aug 15. PMID:22896702<ref>PMID:22896702</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: Abramson, J | [[Category: Abramson, J]] | ||
[[Category: Dahlquist, F W | [[Category: Dahlquist, F W]] | ||
[[Category: Fortgang, E A | [[Category: Fortgang, E A]] | ||
[[Category: Paz, A | [[Category: Paz, A]] | ||
[[Category: Vartanian, A S | [[Category: Vartanian, A S]] | ||
[[Category: Flagellar motor]] | [[Category: Flagellar motor]] | ||
[[Category: Motor protein]] | [[Category: Motor protein]] | ||
Revision as of 18:02, 9 December 2014
Crystal structure of the complex between the flagellar motor proteins FliG and FliM.Crystal structure of the complex between the flagellar motor proteins FliG and FliM.
Structural highlights
Publication Abstract from PubMedThe flagellar motor is one type of propulsion device of motile bacteria. The cytoplasmic ring (C-ring) of the motor interacts with the stator to generate torque in clockwise and counterclockwise directions. The C-ring is composed of three proteins, FliM, FliN, and FliG. Together they form the "switch complex" and regulate switching and torque generation. Here we report the crystal structure of the middle domain of FliM in complex with the middle and C-terminal domains of FliG that shows the interaction surface and orientations of the proteins. In the complex, FliG assumes a compact conformation in which the middle and C-terminal domains (FliG(MC)) collapse and stack together similarly to the recently published structure of a mutant of FliG(MC) with a clockwise rotational bias. This intramolecular stacking of the domains is distinct from the intermolecular stacking seen in other structures of FliG. We fit the complex structure into the three-dimensional reconstructions of the motor and propose that the cytoplasmic ring is assembled from 34 FliG and FliM molecules in a 1:1 fashion. Structure of flagellar motor proteins in complex allows for insights into motor structure and switching.,Vartanian AS, Paz A, Fortgang EA, Abramson J, Dahlquist FW J Biol Chem. 2012 Oct 19;287(43):35779-83. doi: 10.1074/jbc.C112.378380. Epub, 2012 Aug 15. PMID:22896702[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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