1n12: Difference between revisions

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-{{Seed}}
-[[Image:1n12.png|left|200px]]
-<!--
+==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==
-The line below this paragraph, containing "STRUCTURE_1n12", creates the "Structure Box" on the page.
+<StructureSection load='1n12' size='340' side='right'caption='[[1n12]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87&#8491;</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>
-{{STRUCTURE_1n12|  PDB=1n12  |  SCENE=  }}
+<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.
-===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===
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_12437927}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1n12" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 12437927 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_12437927}}
+__TOC__
+</StructureSection>
-==About this Structure==
-N12 is a 4 chains structure of sequences from [http://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].
-==Reference==
-<ref group="xtra">PMID:12437927</ref><references group="xtra"/>
 [[Category: Escherichia coli]]
-[[Category: Hultgren, S J.]]
+[[Category: Large Structures]]
-[[Category: Pinkner, J S.]]
+[[Category: Hultgren SJ]]
-[[Category: Sauer, F G.]]
+[[Category: Pinkner JS]]
-[[Category: Waksman, G.]]
+[[Category: Sauer FG]]
-[[Category: Chaperone priming]]
+[[Category: Waksman G]]
-[[Category: Donor strand complementation]]
-[[Category: Donor strand exchange]]
-[[Category: Immunoglobulin-like fold]]
-[[Category: Organelle biogenesis]]
-[[Category: Pilus fiber assembly]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 20:09:30 2009''