3s0h

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Current revision (09:46, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3s0h' size='340' side='right'caption='[[3s0h]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3s0h' size='340' side='right'caption='[[3s0h]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3s0h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S0H FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3s0h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S0H FirstGlance]. <br>
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</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>
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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]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3s02|3s02]], [[3s03|3s03]], [[3s06|3s06]], [[3s0w|3s0w]], [[3s0y|3s0y]]</div></td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">motB, HP_0816 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</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=3s0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s0h OCA], [https://pdbe.org/3s0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s0h RCSB], [https://www.ebi.ac.uk/pdbsum/3s0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s0h 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=3s0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s0h OCA], [https://pdbe.org/3s0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s0h RCSB], [https://www.ebi.ac.uk/pdbsum/3s0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s0h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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).
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3s0h" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43504]]
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[[Category: Helicobacter pylori]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Roujeinikova, A R]]
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[[Category: Roujeinikova AR]]
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[[Category: Bacterial flagellar motor]]
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[[Category: Chemotaxis]]
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[[Category: Flagellar rotation]]
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[[Category: Membrane]]
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[[Category: Motor protein]]
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[[Category: Peptidoglycan binding]]
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Current revision

The crystal structure of the periplasmic domain of Helicobacter pylori MotB (residues 90-256).

PDB ID 3s0h

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