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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BY4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5by4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://oca.weizmann.ac.il/oca-docs/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> | </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='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=5by4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5by4 OCA], [http://pdbe.org/5by4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5by4 RCSB], [http://www.ebi.ac.uk/pdbsum/5by4 PDBsum]</span></td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tolR, b0738, JW0728 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=5by4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5by4 OCA], [http://pdbe.org/5by4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5by4 RCSB], [http://www.ebi.ac.uk/pdbsum/5by4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5by4 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | |||
[[Category: Kaminska, R]] | [[Category: Kaminska, R]] | ||
[[Category: Kleanthous, C]] | [[Category: Kleanthous, C]] | ||
Revision as of 17:42, 16 November 2017
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
Function[TOLR_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. References
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