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3ajc

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<StructureSection load='3ajc' size='340' side='right'caption='[[3ajc]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3ajc' size='340' side='right'caption='[[3ajc]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ajc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AJC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ajc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AJC FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fliG, TM_0220 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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]] 2.3&#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=3ajc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ajc OCA], [https://pdbe.org/3ajc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ajc RCSB], [https://www.ebi.ac.uk/pdbsum/3ajc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ajc 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=3ajc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ajc OCA], [https://pdbe.org/3ajc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ajc RCSB], [https://www.ebi.ac.uk/pdbsum/3ajc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ajc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/FLIG_THEMA FLIG_THEMA]] One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
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[https://www.uniprot.org/uniprot/FLIG_THEMA FLIG_THEMA] One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The bacterial flagellar motor can rotate either clockwise (CW) or counterclockwise (CCW). Three flagellar proteins, FliG, FliM, and FliN, are required for rapid switching between the CW and CCW directions. Switching is achieved by a conformational change in FliG induced by the binding of a chemotaxis signaling protein, phospho-CheY, to FliM and FliN. FliG consists of three domains, FliG(N), FliG(M), and FliG(C), and forms a ring on the cytoplasmic face of the MS ring of the flagellar basal body. Crystal structures have been reported for the FliG(MC) domains of Thermotoga maritima, which consist of the FliG(M) and FliG(C) domains and a helix E that connects these two domains, and full-length FliG of Aquifex aeolicus. However, the basis for the switching mechanism is based only on previously obtained genetic data and is hence rather indirect. We characterized a CW-biased mutant (fliG(DeltaPAA)) of Salmonella enterica by direct observation of rotation of a single motor at high temporal and spatial resolution. We also determined the crystal structure of the FliG(MC) domains of an equivalent deletion mutant variant of T. maritima (fliG(DeltaPEV)). The FliG(DeltaPAA) motor produced torque at wild-type levels under a wide range of external load conditions. The wild-type motors rotated exclusively in the CCW direction under our experimental conditions, whereas the mutant motors rotated only in the CW direction. This result suggests that wild-type FliG is more stable in the CCW state than in the CW state, whereas FliG(DeltaPAA) is more stable in the CW state than in the CCW state. The structure of the TM-FliG(MC)(DeltaPEV) revealed that extremely CW-biased rotation was caused by a conformational change in helix E. Although the arrangement of FliG(C) relative to FliG(M) in a single molecule was different among the three crystals, a conserved FliG(M)-FliG(C) unit was observed in all three of them. We suggest that the conserved FliG(M)-FliG(C) unit is the basic functional element in the rotor ring and that the PAA deletion induces a conformational change in a hinge-loop between FliG(M) and helix E to achieve the CW state of the FliG ring. We also propose a novel model for the arrangement of FliG subunits within the motor. The model is in agreement with the previous mutational and cross-linking experiments and explains the cooperative switching mechanism of the flagellar motor.
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Structural insight into the rotational switching mechanism of the bacterial flagellar motor.,Minamino T, Imada K, Kinoshita M, Nakamura S, Morimoto YV, Namba K PLoS Biol. 2011 May;9(5):e1000616. doi: 10.1371/journal.pbio.1000616. Epub 2011, May 10. PMID:21572987<ref>PMID:21572987</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 3ajc" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43589]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Imada, K]]
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[[Category: Thermotoga maritima]]
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[[Category: Kinoshita, M]]
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[[Category: Imada K]]
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[[Category: Minamino, T]]
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[[Category: Kinoshita M]]
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[[Category: Namba, K]]
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[[Category: Minamino T]]
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[[Category: Chemotaxis]]
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[[Category: Namba K]]
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[[Category: Flagellar motor]]
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[[Category: Flagellum]]
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[[Category: Structural protein]]
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Current revision

Structure of the MC domain of FliG (PEV), a CW-biased mutant

PDB ID 3ajc

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