5by4: Difference between revisions
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==Structure and function of the Escherichia coli Tol-Pal stator protein TolR== | ==Structure and function of the Escherichia coli Tol-Pal stator protein TolR== | ||
<StructureSection load='5by4' size='340' side='right' caption='[[5by4]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5by4' size='340' side='right'caption='[[5by4]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5by4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5by4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BY4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BY4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=5by4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5by4 OCA], [https://pdbe.org/5by4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5by4 RCSB], [https://www.ebi.ac.uk/pdbsum/5by4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5by4 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/TOLR_ECOLI TOLR_ECOLI] Involved in the TonB-independent uptake of group A colicins (colicins A, E1, E2, E3, and K). | ||
<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 5by4" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5by4" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[TolR|TolR]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Kaminska R]] | ||
[[Category: | [[Category: Kleanthous C]] | ||
[[Category: | [[Category: Wojdyla JA]] | ||
Revision as of 09:12, 7 June 2023
Structure and function of the Escherichia coli Tol-Pal stator protein TolRStructure and function of the Escherichia coli Tol-Pal stator protein TolR
Structural highlights
FunctionTOLR_ECOLI Involved in the TonB-independent uptake of group A colicins (colicins A, E1, E2, E3, and K). Publication Abstract from PubMedTolR is a 15-kDa inner membrane protein subunit of the Tol-Pal complex in Gram- negative bacteria the function of which is poorly understood. Tol-Pal is recruited to cell division sites where it is involved in maintaining the integrity of the outer membrane. TolR is related to MotB, the peptidoglycan (PG)-binding stator protein from the flagellum, suggesting it might serve a similar role in Tol-Pal. The only structure thus far reported for TolR is of the periplasmic domain from Haemophilus influenzae in which N- and C-terminal residues had been deleted (TolR62-133, E. coli numbering). H. influenzae TolR62-133 is a symmetrical dimer with a large deep cleft at the dimer interface. Here, we present the 1.7 A crystal structure of the intact periplasmic domain of Escherichia coli TolR (TolR36-142). E. coli TolR36-142 is also dimeric but the architecture of the dimer is radically different to that of TolR62-133 due to intertwining of its N- and C-termini. TolR monomers are rotated ~180 degrees relative to each other as a result of this strand-swapping, obliterating the putative PG-binding groove seen in TolR62-133. We found that removal of the strand swapped regions (TolR60-133) exposes cryptic PG binding activity that is absent in the full-length domain. We conclude that to function as a stator in the Tol-Pal complex dimeric TolR must undergo large- scale structural remodelling reminiscent of that proposed for MotB where N- and C-terminal sequences unfold in order for the protein to both reach and bind the PG layer ~90 A away from the inner membrane. Structure and Function of the Escherichia coli Tol-Pal Stator Protein TolR.,Wojdyla JA, Cutts E, Kaminska R, Papadakos G, Hopper JT, Stansfeld PJ, Staunton D, Robinson CV, Kleanthous C J Biol Chem. 2015 Sep 9. pii: jbc.M115.671586. PMID:26354441[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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