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3s03

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The crystal structure of the periplasmic domain of Helicobacter pylori MotB (residues 97-256, P43).

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Retrieved from "http://52.214.119.220/wiki/index.php/3s03"

Categories: Helicobacter pylori 26695 | Large Structures | Roujeinikova AR

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 <StructureSection load='3s03' size='340' side='right'caption='[[3s03]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3s03]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S03 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3s03]] is a 4 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=3S03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S03 FirstGlance]. <br>
-</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>
+</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"><div style='overflow: auto; max-height: 3em;'>[[3s02|3s02]], [[3s06|3s06]], [[3s0h|3s0h]], [[3s0w|3s0w]], [[3s0y|3s0y]]</div></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 ([https://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=3s03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s03 OCA], [https://pdbe.org/3s03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s03 RCSB], [https://www.ebi.ac.uk/pdbsum/3s03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s03 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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).
+[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 3s03" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Campylobacter pylori]]
+[[Category: Helicobacter pylori 26695]]
 [[Category: Large Structures]]
-[[Category: Roujeinikova, A R]]
+[[Category: Roujeinikova AR]]
-[[Category: Bacterial flagellar motor]]
-[[Category: Chemotaxis]]
-[[Category: Flagellar rotation]]
-[[Category: Membrane]]
-[[Category: Motor protein]]
-[[Category: Peptidoglycan binding]]

3s03

From Proteopedia

Current revision

The crystal structure of the periplasmic domain of Helicobacter pylori MotB (residues 97-256, P43).

Structural highlights

Function

See Also

Contents

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