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==The crystal structure of the periplasmic domain of Helicobacter pylori MotB (residues 78-256).==
==The crystal structure of the periplasmic domain of Helicobacter pylori MotB (residues 78-256).==
<StructureSection load='3s0w' size='340' side='right' caption='[[3s0w]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3s0w' size='340' side='right'caption='[[3s0w]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3s0w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S0W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S0W FirstGlance]. <br>
<table><tr><td colspan='2'>[[3s0w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S0W FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3s02|3s02]], [[3s03|3s03]], [[3s06|3s06]], [[3s0h|3s0h]], [[3s0y|3s0y]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP_0816, motB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</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=3s0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s0w OCA], [https://pdbe.org/3s0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s0w RCSB], [https://www.ebi.ac.uk/pdbsum/3s0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s0w 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=3s0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s0w OCA], [http://pdbe.org/3s0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3s0w RCSB], [http://www.ebi.ac.uk/pdbsum/3s0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3s0w ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MOTB_HELPY MOTB_HELPY]] 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_HELPY MOTB_HELPY] 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;">
== Publication Abstract from PubMed ==
Bacterial flagella are driven by an ion influx through the peptidoglycan (PG)-tethered MotA/MotB stator. Stator precomplexes assemble in the membrane and remain inactive until they incorporate into the motor, upon which MotA/MotB changes conformation. The nature of this change and the mechanism of inhibition of the PG-binding and ion-conducting activities of the precomplexes are unknown. Here, the structural analysis of a series of N-terminally truncated MotB fragments is presented, the mechanism of inhibition by the linker is identified and the structural basis for the formation of the PG-binding-competent open-channel MotA/MotB conformation via a mechanism that entails linker unfolding and rotational displacement of MotB transmembrane helices is uncovered.
 
Role of the MotB linker in the assembly and activation of the bacterial flagellar motor.,O'Neill J, Xie M, Hijnen M, Roujeinikova A Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1009-16. Epub 2011 Nov 5. PMID:22120737<ref>PMID:22120737</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3s0w" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Chemotaxis protein|Chemotaxis protein]]
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Campylobacter pylori]]
[[Category: Helicobacter pylori 26695]]
[[Category: Roujeinikova, A R]]
[[Category: Large Structures]]
[[Category: Bacterial flagellar motor]]
[[Category: Roujeinikova AR]]
[[Category: Chemotaxis]]
[[Category: Flagellar rotation]]
[[Category: Membrane]]
[[Category: Motor protein]]
[[Category: Peptidoglycan binding]]
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