3soh: Difference between revisions

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 <StructureSection load='3soh' size='340' side='right'caption='[[3soh]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3soh]] is a 4 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=3SOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SOH FirstGlance]. <br>
+<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>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hp7|2hp7]], [[1lkv|1lkv]]</div></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]] 3.5&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_0679 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589]), fliG, TM_0220 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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=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>
 </table>
 == Function ==
-[[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). [[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).
+[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).
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3soh" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Flagellar protein 3D structures|Flagellar protein 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 43589]]
 [[Category: Large Structures]]
-[[Category: Bilwes, A M]]
+[[Category: Thermotoga maritima]]
-[[Category: Blair, D]]
+[[Category: Bilwes AM]]
-[[Category: Crane, B R]]
+[[Category: Blair D]]
-[[Category: Gonzalez-Bonet, G]]
+[[Category: Crane BR]]
-[[Category: Koushik, P]]
+[[Category: Gonzalez-Bonet G]]
-[[Category: Alpha/beta]]
+[[Category: Koushik P]]
-[[Category: Motor protein]]
-[[Category: Protein-protein complex]]