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| | ==Structure of the periplasmic domain of the MotB L119P mutant from Salmonella (crystal form 2)== | | ==Structure of the periplasmic domain of the MotB L119P mutant from Salmonella (crystal form 2)== |
| - | <StructureSection load='5y40' size='340' side='right' caption='[[5y40]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='5y40' size='340' side='right'caption='[[5y40]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5y40]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y40 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y40 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5y40]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y40 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zov|2zov]], [[2zvy|2zvy]], [[2zvz|2zvz]], [[5y3z|5y3z]]</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]] 2.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">motB, STM1922 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</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=5y40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y40 OCA], [https://pdbe.org/5y40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y40 RCSB], [https://www.ebi.ac.uk/pdbsum/5y40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y40 ProSAT]</span></td></tr> |
| - | <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=5y40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y40 OCA], [http://pdbe.org/5y40 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y40 RCSB], [http://www.ebi.ac.uk/pdbsum/5y40 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y40 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MOTB_SALTY MOTB_SALTY]] MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity). | + | [https://www.uniprot.org/uniprot/MOTB_SALTY MOTB_SALTY] MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5y40" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5y40" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Salty]] | + | [[Category: Large Structures]] |
| - | [[Category: Homma, M]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] |
| - | [[Category: Imada, K]] | + | [[Category: Homma M]] |
| - | [[Category: Kojima, S]] | + | [[Category: Imada K]] |
| - | [[Category: Sakuma, M]] | + | [[Category: Kojima S]] |
| - | [[Category: Takao, M]] | + | [[Category: Sakuma M]] |
| - | [[Category: 2-layer sandwich]]
| + | [[Category: Takao M]] |
| - | [[Category: Bacterial flagellum]]
| + | |
| - | [[Category: Cell projection]]
| + | |
| - | [[Category: Chemotaxis]]
| + | |
| - | [[Category: Flagellar rotation]]
| + | |
| - | [[Category: Inner membrane]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Motor protein]]
| + | |
| Structural highlights
Function
MOTB_SALTY MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity).
Publication Abstract from PubMed
The stator of the bacterial flagellar motor couples ion flow with torque generation. The ion-conducting stator channel opens only when incorporated into and anchored around the rotor via the peptidoglycan (PG) binding domain of the B subunit (MotBC). However, no direct evidence of PG binding coupled with channel activation has been presented. Here, we report the structural rearrangements of MotBC responsible for this coupling process. A MotBC fragment with the L119P replacement, which is known to cause channel activation, was able to bind PG. Nuclear magnetic resonance analysis of MotBC and the crystal structure of the MotBC-L119P dimer revealed major structural changes in helix alpha1. In vivo crosslinking results confirm that a major rearrangement occurs. Our results suggest that, upon stator incorporation into the motor, helix alpha1 of MotBC changes into an extended non-helical structure. We propose that this change allows the stator both to bind PG and to open its proton channel.
The Helix Rearrangement in the Periplasmic Domain of the Flagellar Stator B Subunit Activates Peptidoglycan Binding and Ion Influx.,Kojima S, Takao M, Almira G, Kawahara I, Sakuma M, Homma M, Kojima C, Imada K Structure. 2018 Apr 3;26(4):590-598.e5. doi: 10.1016/j.str.2018.02.016. Epub 2018, Mar 22. PMID:29576320[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kojima S, Takao M, Almira G, Kawahara I, Sakuma M, Homma M, Kojima C, Imada K. The Helix Rearrangement in the Periplasmic Domain of the Flagellar Stator B Subunit Activates Peptidoglycan Binding and Ion Influx. Structure. 2018 Apr 3;26(4):590-598.e5. doi: 10.1016/j.str.2018.02.016. Epub 2018, Mar 22. PMID:29576320 doi:http://dx.doi.org/10.1016/j.str.2018.02.016
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