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==Crystal structure of the PapE (N-terminal-deleted) pilus subunit bound to a peptide corresponding to the N-terminal extension of the PapK pilus subunit (residues 1-11) from uropathogenic E. coli== | |||
<StructureSection load='1n12' size='340' side='right'caption='[[1n12]], [[Resolution|resolution]] 1.87Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1n12]] is a 4 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=1N12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N12 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]] 1.87Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1n12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n12 OCA], [https://pdbe.org/1n12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n12 RCSB], [https://www.ebi.ac.uk/pdbsum/1n12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n12 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PAPE_ECOLX PAPE_ECOLX] Repeated PapE subunits make up the thin (2 nm in diameter) tip fibrillum of the pilus. Subunits are arranged in a open helical conformation. Pili with a defective papE gene have low adhesive capacity or none; however, the binding property of the whole cell is not affected. Pili are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, and enable bacteria to colonize the epithelium of specific host organs. | |||
== 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/n1/1n12_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1n12 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Periplasmic chaperones direct the assembly of adhesive, multi-subunit pilus fibers that play critical roles in bacterial pathogenesis. Pilus assembly occurs via a donor strand exchange mechanism in which the N-terminal extension of one subunit replaces the chaperone G(1) strand that transiently occupies a groove in the neighboring subunit. Here, we show that the chaperone primes the subunit for assembly by holding the groove in an open, activated conformation. During donor strand exchange, the subunit undergoes a topological transition that triggers the closure of the groove and seals the N-terminal extension in place. It is this topological transition, made possible only by the priming action of the chaperone that drives subunit assembly into the fiber. | Periplasmic chaperones direct the assembly of adhesive, multi-subunit pilus fibers that play critical roles in bacterial pathogenesis. Pilus assembly occurs via a donor strand exchange mechanism in which the N-terminal extension of one subunit replaces the chaperone G(1) strand that transiently occupies a groove in the neighboring subunit. Here, we show that the chaperone primes the subunit for assembly by holding the groove in an open, activated conformation. During donor strand exchange, the subunit undergoes a topological transition that triggers the closure of the groove and seals the N-terminal extension in place. It is this topological transition, made possible only by the priming action of the chaperone that drives subunit assembly into the fiber. | ||
Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation.,Sauer FG, Pinkner JS, Waksman G, Hultgren SJ Cell. 2002 Nov 15;111(4):543-51. PMID:12437927<ref>PMID:12437927</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1n12" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Hultgren | [[Category: Hultgren SJ]] | ||
[[Category: Pinkner | [[Category: Pinkner JS]] | ||
[[Category: Sauer | [[Category: Sauer FG]] | ||
[[Category: Waksman | [[Category: Waksman G]] | ||
Latest revision as of 10:22, 9 October 2024
Crystal structure of the PapE (N-terminal-deleted) pilus subunit bound to a peptide corresponding to the N-terminal extension of the PapK pilus subunit (residues 1-11) from uropathogenic E. coliCrystal structure of the PapE (N-terminal-deleted) pilus subunit bound to a peptide corresponding to the N-terminal extension of the PapK pilus subunit (residues 1-11) from uropathogenic E. coli
Structural highlights
FunctionPAPE_ECOLX Repeated PapE subunits make up the thin (2 nm in diameter) tip fibrillum of the pilus. Subunits are arranged in a open helical conformation. Pili with a defective papE gene have low adhesive capacity or none; however, the binding property of the whole cell is not affected. Pili are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, and enable bacteria to colonize the epithelium of specific host organs. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPeriplasmic chaperones direct the assembly of adhesive, multi-subunit pilus fibers that play critical roles in bacterial pathogenesis. Pilus assembly occurs via a donor strand exchange mechanism in which the N-terminal extension of one subunit replaces the chaperone G(1) strand that transiently occupies a groove in the neighboring subunit. Here, we show that the chaperone primes the subunit for assembly by holding the groove in an open, activated conformation. During donor strand exchange, the subunit undergoes a topological transition that triggers the closure of the groove and seals the N-terminal extension in place. It is this topological transition, made possible only by the priming action of the chaperone that drives subunit assembly into the fiber. Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation.,Sauer FG, Pinkner JS, Waksman G, Hultgren SJ Cell. 2002 Nov 15;111(4):543-51. PMID:12437927[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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