3hjl: Difference between revisions

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 ==The structure of full-length FliG from Aquifex aeolicus==
-<StructureSection load='3hjl' size='340' side='right' caption='[[3hjl]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='3hjl' size='340' side='right'caption='[[3hjl]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3hjl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HJL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3hjl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HJL FirstGlance]. <br>
-</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=3hjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hjl OCA], [http://pdbe.org/3hjl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hjl RCSB], [http://www.ebi.ac.uk/pdbsum/3hjl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hjl ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=3hjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hjl OCA], [https://pdbe.org/3hjl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hjl RCSB], [https://www.ebi.ac.uk/pdbsum/3hjl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hjl ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/FLIG_AQUAE FLIG_AQUAE]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 16: / Line 19: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hjl ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The flagellar motor drives the rotation of flagellar filaments at hundreds of revolutions per second, efficiently propelling bacteria through viscous media. The motor uses the potential energy from an electrochemical gradient of cations across the cytoplasmic membrane to generate torque. A rapid switch from anticlockwise to clockwise rotation determines whether a bacterium runs smoothly forward or tumbles to change its trajectory. A protein called FliG forms a ring in the rotor of the flagellar motor that is involved in the generation of torque through an interaction with the cation-channel-forming stator subunit MotA. FliG has been suggested to adopt distinct conformations that induce switching but these structural changes and the molecular mechanism of switching are unknown. Here we report the molecular structure of the full-length FliG protein, identify conformational changes that are involved in rotational switching and uncover the structural basis for the formation of the FliG torque ring. This allows us to propose a model of the complete ring and switching mechanism in which conformational changes in FliG reverse the electrostatic charges involved in torque generation.
-Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching.,Lee LK, Ginsburg MA, Crovace C, Donohoe M, Stock D Nature. 2010 Aug 19;466(7309):996-1000. Epub 2010 Aug 1. PMID:20676082<ref>PMID:20676082</ref>
+==See Also==
+*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3hjl" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Aquifex aeolicus huber and stetter 2001]]
+[[Category: Aquifex aeolicus]]
-[[Category: Crovace, C]]
+[[Category: Large Structures]]
-[[Category: Donohoe, M]]
+[[Category: Crovace C]]
-[[Category: Ginsburg, M A]]
+[[Category: Donohoe M]]
-[[Category: Lee, L K]]
+[[Category: Ginsburg MA]]
-[[Category: Stock, D]]
+[[Category: Lee LK]]
-[[Category: Armadillo repeat motif]]
+[[Category: Stock D]]
-[[Category: Bacterial flagellar motor]]
-[[Category: Bacterial flagellum]]
-[[Category: Biological energy conversion]]
-[[Category: Cell inner membrane]]
-[[Category: Cell membrane]]
-[[Category: Chemotaxis]]
-[[Category: Conformational plasticity]]
-[[Category: Flagellar rotation]]
-[[Category: Fold repeat]]
-[[Category: Membrane]]
-[[Category: Proton transport]]
-[[Category: Rotary motor]]
-[[Category: Superhelix]]
-[[Category: Switch complex]]
-[[Category: Torque generation]]