3hjl: Difference between revisions
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==The structure of full-length FliG from Aquifex aeolicus== | ==The structure of full-length FliG from Aquifex aeolicus== | ||
<StructureSection load='3hjl' size='340' side='right' caption='[[3hjl]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3hjl' size='340' side='right'caption='[[3hjl]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == 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:// | <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://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:// | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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</div> | </div> | ||
<div class="pdbe-citations 3hjl" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3hjl" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Aquifex aeolicus huber and stetter 2001]] | [[Category: Aquifex aeolicus huber and stetter 2001]] | ||
[[Category: Large Structures]] | |||
[[Category: Crovace, C]] | [[Category: Crovace, C]] | ||
[[Category: Donohoe, M]] | [[Category: Donohoe, M]] | ||
Revision as of 13:48, 16 September 2020
The structure of full-length FliG from Aquifex aeolicusThe structure of full-length FliG from Aquifex aeolicus
Structural highlights
Evolutionary 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 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Aquifex aeolicus huber and stetter 2001
- Large Structures
- Crovace, C
- Donohoe, M
- Ginsburg, M A
- Lee, L K
- Stock, D
- Armadillo repeat motif
- Bacterial flagellar motor
- Bacterial flagellum
- Biological energy conversion
- Cell inner membrane
- Cell membrane
- Chemotaxis
- Conformational plasticity
- Flagellar rotation
- Fold repeat
- Membrane
- Proton transport
- Rotary motor
- Superhelix
- Switch complex
- Torque generation