3soh

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==Architecture of the Flagellar Rotor==
==Architecture of the Flagellar Rotor==
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<StructureSection load='3soh' size='340' side='right' caption='[[3soh]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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<StructureSection load='3soh' size='340' side='right'caption='[[3soh]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3soh]] is a 4 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=3SOH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SOH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3soh]] is a 4 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=3SOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SOH FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hp7|2hp7]], [[1lkv|1lkv]]</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]] 3.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_0679 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]), fliG, TM_0220 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</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=3soh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3soh OCA], [https://pdbe.org/3soh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3soh RCSB], [https://www.ebi.ac.uk/pdbsum/3soh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3soh ProSAT]</span></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=3soh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3soh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3soh RCSB], [http://www.ebi.ac.uk/pdbsum/3soh PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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/FLIM_THEMA FLIM_THEMA] FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheX chemotaxis proteins, 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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Rotation and switching of the bacterial flagellum depends on a large rotor-mounted protein assembly composed of the proteins FliG, FliM and FliN, with FliG most directly involved in rotation. The crystal structure of a complex between the central domains of FliG and FliM, in conjunction with several biochemical and molecular-genetic experiments, reveals the arrangement of the FliG and FliM proteins in the rotor. A stoichiometric mismatch between FliG (26 subunits) and FliM (34 subunits) is explained in terms of two distinct positions for FliM: one where it binds the FliG central domain and another where it binds the FliG C-terminal domain. This architecture provides a structural framework for addressing the mechanisms of motor rotation and direction switching and for unifying the large body of data on motor performance. Recently proposed alternative models of rotor assembly, based on a subunit contact observed in crystals, are not supported by experiment.
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Architecture of the flagellar rotor.,Paul K, Gonzalez-Bonet G, Bilwes AM, Crane BR, Blair D EMBO J. 2011 Jun 14;30(14):2962-71. doi: 10.1038/emboj.2011.188. PMID:21673656<ref>PMID:21673656</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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==See Also==
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</div>
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*[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Bilwes, A M]]
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[[Category: Bilwes AM]]
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[[Category: Blair, D]]
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[[Category: Blair D]]
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[[Category: Crane, B R]]
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[[Category: Crane BR]]
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[[Category: Gonzalez-Bonet, G]]
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[[Category: Gonzalez-Bonet G]]
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[[Category: Koushik, P]]
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[[Category: Koushik P]]
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[[Category: Alpha/beta]]
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[[Category: Motor protein]]
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[[Category: Protein-protein complex]]
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Current revision

Architecture of the Flagellar Rotor

PDB ID 3soh

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