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| | <StructureSection load='7dm9' size='340' side='right'caption='[[7dm9]], [[Resolution|resolution]] 1.71Å' scene=''> | | <StructureSection load='7dm9' size='340' side='right'caption='[[7dm9]], [[Resolution|resolution]] 1.71Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7dm9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"oceanomonas_alginolytica"_miyamoto_et_al._1961 "oceanomonas alginolytica" miyamoto et al. 1961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DM9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7dm9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_alginolyticus Vibrio alginolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DM9 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Vag1382_20640, VagVIO5_20640, VagYM19_20670, VagYM4_20660 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=663 "Oceanomonas alginolytica" Miyamoto et al. 1961])</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]] 1.71Å</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=7dm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dm9 OCA], [https://pdbe.org/7dm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dm9 RCSB], [https://www.ebi.ac.uk/pdbsum/7dm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dm9 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=7dm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dm9 OCA], [https://pdbe.org/7dm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dm9 RCSB], [https://www.ebi.ac.uk/pdbsum/7dm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dm9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/A0A6F8W0A1_VIBAL A0A6F8W0A1_VIBAL]] 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 CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.[PIRNR:PIRNR002888]
| + | [https://www.uniprot.org/uniprot/A0A1W6VDB9_VIBAL A0A1W6VDB9_VIBAL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Oceanomonas alginolytica miyamoto et al. 1961]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Homma, M]] | + | [[Category: Vibrio alginolyticus]] |
| - | [[Category: Imada, K]] | + | [[Category: Homma M]] |
| - | [[Category: Takekawa, N]] | + | [[Category: Imada K]] |
| - | [[Category: Flagellar motor protein]] | + | [[Category: Takekawa N]] |
| - | [[Category: Motor protein]]
| + | |
| Structural highlights
Function
A0A1W6VDB9_VIBAL
Publication Abstract from PubMed
Many bacteria swim by rotating flagella. The chemotaxis system controls the direction of flagellar rotation. Vibrio alginolyticus, which has a single polar flagellum, swims smoothly by rotating the flagellar motor counterclockwise (CCW) in response to attractants. In response to repellents, the motor frequently switches its rotational direction between CCW and clockwise (CW). We isolated a mutant strain that swims with a CW-locked rotation of the flagellum, which pulls rather than pushes the cell. This CW phenotype arises from a R49P substitution in FliM, which is the component in the C-ring of the motor that binds the chemotaxis signaling protein, phosphorylated CheY. However, this phenotype is independent of CheY, indicating that the mutation produces a CW conformation of the C-ring in the absence of CheY. The crystal structure of FliM with the R49P substitution showed a conformational change in the N-terminal alpha-helix of the middle domain of FliM (FliMM). This helix should mediates FliM-FliM interaction. The structural models of wild-type and mutant C-ring showed that the relatively small conformational change in FliMM induces a drastic rearrangement of the conformation of the FliMM domain that generates a CW conformation of the C-ring.
A slight bending of an alpha-helix in FliM creates a counterclockwise-locked structure of the flagellar motor in Vibrio.,Takekawa N, Nishikino T, Yamashita T, Hori K, Onoue Y, Ihara K, Kojima S, Homma M, Imada K J Biochem. 2021 Jun 18. pii: 6304869. doi: 10.1093/jb/mvab074. PMID:34143212[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Takekawa N, Nishikino T, Yamashita T, Hori K, Onoue Y, Ihara K, Kojima S, Homma M, Imada K. A slight bending of an alpha-helix in FliM creates a counterclockwise-locked structure of the flagellar motor in Vibrio. J Biochem. 2021 Jun 18. pii: 6304869. doi: 10.1093/jb/mvab074. PMID:34143212 doi:http://dx.doi.org/10.1093/jb/mvab074
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