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==The crystal structure of the periplasmic domain of Helicobacter pylori MotB (residues 90-256).==
==The crystal structure of the periplasmic domain of Helicobacter pylori MotB (residues 90-256).==
<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 ==
<table><tr><td colspan='2'>[[3s0h]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3S0H FirstGlance]. <br>
<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>
</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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3s02|3s02]], [[3s03|3s03]], [[3s06|3s06]], [[3s0w|3s0w]], [[3s0y|3s0y]]</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]], [[3s03|3s03]], [[3s06|3s06]], [[3s0w|3s0w]], [[3s0y|3s0y]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">motB, HP_0816 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr>
<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>
<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=3s0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s0h OCA], [http://pdbe.org/3s0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3s0h RCSB], [http://www.ebi.ac.uk/pdbsum/3s0h PDBsum], [http://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 ==
[[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Chemotaxis protein|Chemotaxis protein]]
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Atcc 43504]]
[[Category: Atcc 43504]]
[[Category: Large Structures]]
[[Category: Roujeinikova, A R]]
[[Category: Roujeinikova, A R]]
[[Category: Bacterial flagellar motor]]
[[Category: Bacterial flagellar motor]]

Revision as of 13:32, 22 June 2022

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

Structural highlights

3s0h is a 4 chain structure with sequence from Atcc 43504. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:motB, HP_0816 (ATCC 43504)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. O'Neill J, Xie M, Hijnen M, Roujeinikova A. Role of the MotB linker in the assembly and activation of the bacterial flagellar motor. Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1009-16. Epub 2011 Nov 5. PMID:22120737 doi:10.1107/S0907444911041102

3s0h, resolution 2.10Å

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