4fq0: Difference between revisions
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==Crystal structure of FliG-FliM complex from H. pylori== | ==Crystal structure of FliG-FliM complex from H. pylori== | ||
<StructureSection load='4fq0' size='340' side='right' caption='[[4fq0]], [[Resolution|resolution]] 2.82Å' scene=''> | <StructureSection load='4fq0' size='340' side='right'caption='[[4fq0]], [[Resolution|resolution]] 2.82Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fq0]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4fq0]] 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=4FQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FQ0 FirstGlance]. <br> | ||
</td></tr> | </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=4fq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fq0 OCA], [https://pdbe.org/4fq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fq0 RCSB], [https://www.ebi.ac.uk/pdbsum/4fq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fq0 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/O25675_HELPY O25675_HELPY] | ||
<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 4fq0" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4fq0" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Helicobacter pylori 26695]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Au SWN]] | ||
[[Category: | [[Category: Lam KH]] | ||
Revision as of 23:04, 19 October 2022
Crystal structure of FliG-FliM complex from H. pyloriCrystal structure of FliG-FliM complex from H. pylori
Structural highlights
FunctionPublication Abstract from PubMedFliG and FliM are switch proteins that regulate the rotation and switching of the flagellar motor. Several assembly models for FliG and FliM have recently been proposed; however, it remains unclear whether the assembly of the switch proteins is conserved among different bacterial species. We applied a combination of pull-down, thermodynamic and structural analyses to characterize the FliM-FliG association from the mesophilic bacterium Helicobacter pylori. FliM binds to FliG with micromolar binding affinity, and their interaction is mediated through the middle domain of FliG (FliGM ), which contains the EHPQR motif. Crystal structures of the middle domain of H. pylori FliM (FliMM ) and FliGM -FliMM complex revealed that FliG binding triggered a conformational change of the FliM alpha3-alpha1' loop, especially Asp130 and Arg144. We furthermore showed that various highly conserved residues in this region are required for FliM-FliG complex formation. Although the FliM-FliG complex structure displayed a conserved binding mode when compared with Thermotoga maritima, variable residues were identified that may contribute to differential binding affinities across bacterial species. Comparison of the thermodynamic parameters of FliG-FliM interactions between H. pylori and Escherichia coli suggests that molecular basis and binding properties of FliM to FliG is likely different between these two species. Structural basis of FliG-FliM interaction in Helicobacter pylori.,Lam KH, Lam WW, Wong JY, Chan LC, Kotaka M, Ling TK, Jin DY, Ottemann KM, Au SW Mol Microbiol. 2013 Apr 24. doi: 10.1111/mmi.12222. PMID:23614777[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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