2hqs
From Proteopedia
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- | [[Image:2hqs.png|left|200px]] | ||
- | + | ==Crystal structure of TolB/Pal complex== | |
+ | <StructureSection load='2hqs' size='340' side='right'caption='[[2hqs]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2hqs]] is a 8 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=2HQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HQS FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2hqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hqs OCA], [https://pdbe.org/2hqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hqs RCSB], [https://www.ebi.ac.uk/pdbsum/2hqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hqs ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/TOLB_ECOLI TOLB_ECOLI] Involved in the TonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K). Necessary for the colicins to reach their respective targets after initial binding to the bacteria.[HAMAP-Rule:MF_00671] | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hq/2hqs_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hqs ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | We report the crystal structure of the Escherichia coli TolB-Pal complex, a protein-protein complex involved in maintaining the integrity of the outer membrane (OM) in all Gram-negative bacteria that is parasitized by colicins (protein antibiotics) to expedite their entry into cells. Nuclease colicins competitively recruit TolB using their natively disordered regions (NDRs) to disrupt its complex with Pal, which is thought to trigger translocation of the toxin across a locally destabilized OM. The structure shows induced-fit binding of peptidoglycan-associated lipoprotein (Pal) to the beta-propeller domain of TolB causing the N-terminus of one of its alpha-helices to unwind and several residues to undergo substantial changes in conformation. The resulting interactions with TolB are known to be essential for the stability of the complex and the bacterial OM. Structural comparisons with a TolB-colicin NDR complex reveal that colicins bind at the Pal site, mimicking rearranged Pal residues while simultaneously appearing to block induced-fit changes in TolB. The study therefore explains how colicins recruit TolB in the bacterial periplasm and highlights a novel binding mechanism for a natively disordered protein. | ||
- | + | Molecular mimicry enables competitive recruitment by a natively disordered protein.,Bonsor DA, Grishkovskaya I, Dodson EJ, Kleanthous C J Am Chem Soc. 2007 Apr 18;129(15):4800-7. Epub 2007 Mar 22. PMID:17375930<ref>PMID:17375930</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 2hqs" style="background-color:#fffaf0;"></div> | |
- | + | ||
==See Also== | ==See Also== | ||
*[[Pal|Pal]] | *[[Pal|Pal]] | ||
*[[TolB|TolB]] | *[[TolB|TolB]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Bonsor DA]] |
- | [[Category: | + | [[Category: Dodson EJ]] |
- | [[Category: | + | [[Category: Grishkovskaya I]] |
- | [[Category: | + | [[Category: Kleanthous C]] |
- | + | ||
- | + | ||
- | + |
Current revision
Crystal structure of TolB/Pal complex
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