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5vx6

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Current revision (14:12, 13 March 2024) (edit) (undo)
 
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<StructureSection load='5vx6' size='340' side='right'caption='[[5vx6]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='5vx6' size='340' side='right'caption='[[5vx6]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5vx6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VX6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VX6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5vx6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VX6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.197&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ypfA, jofA, BSU22910 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</scene></td></tr>
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<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=5vx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vx6 OCA], [http://pdbe.org/5vx6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vx6 RCSB], [http://www.ebi.ac.uk/pdbsum/5vx6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vx6 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5vx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vx6 OCA], [https://pdbe.org/5vx6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vx6 RCSB], [https://www.ebi.ac.uk/pdbsum/5vx6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vx6 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/YPFA_BACSU YPFA_BACSU]
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Stator elements consisting of MotA4MotB2 complexes are anchored to the cell wall, extend through the cell membrane, and interact with FliG in the cytoplasmic C ring rotor of the flagellum. The cytoplasmic loop of MotA undergoes proton-driven conformational changes that drive flagellar rotation. Functional regulators inhibit motility by either disengaging or jamming the stator-rotor interaction. Here we show that the YcgR homolog MotI (formerly DgrA) of Bacillus subtilis inhibits motility like a molecular clutch that disengages MotA. MotI-inhibited flagella rotated freely by Brownian motion, and suppressor mutations in MotA that were immune to MotI inhibition were located two residues downstream of the critical force generation site. The 3D structure of MotI bound to c-di-GMP was solved, and MotI-fluorescent fusions localized as transient MotA-dependent puncta at the membrane when induced at subinhibitory levels. Finally, subinhibitory levels of MotI expression resulted in incomplete inhibition and proportional decreases in swimming speed. We propose a model in which flagellar stators are disengaged and sequestered from the flagellar rotor when bound by MotI.
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MotI (DgrA) acts as a molecular clutch on the flagellar stator protein MotA in Bacillus subtilis.,Subramanian S, Gao X, Dann CE 3rd, Kearns DB Proc Natl Acad Sci U S A. 2017 Dec 19;114(51):13537-13542. doi:, 10.1073/pnas.1716231114. Epub 2017 Dec 1. PMID:29196522<ref>PMID:29196522</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5vx6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacsu]]
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[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: III, C Dann]]
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[[Category: Dann III C]]
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[[Category: Subramanian, S]]
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[[Category: Subramanian S]]
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[[Category: C-di-gmp]]
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[[Category: Dgra]]
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[[Category: Gmp binding protein]]
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[[Category: Moti]]
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[[Category: Motility]]
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[[Category: Pilz]]
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[[Category: Ycgr]]
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[[Category: Ypfa]]
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Current revision

Structure of Bacillus subtilis Inhibitor of motility (MotI/DgrA)

PDB ID 5vx6

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