2nul: Difference between revisions

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-{{Seed}}
-[[Image:2nul.png|left|200px]]
-<!--
+==PEPTIDYLPROLYL ISOMERASE FROM E. COLI==
-The line below this paragraph, containing "STRUCTURE_2nul", creates the "Structure Box" on the page.
+<StructureSection load='2nul' size='340' side='right'caption='[[2nul]], [[Resolution|resolution]] 2.10&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'>[[2nul]] 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=2NUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NUL 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]] 2.1&#8491;</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=2nul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nul OCA], [https://pdbe.org/2nul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nul RCSB], [https://www.ebi.ac.uk/pdbsum/2nul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nul ProSAT]</span></td></tr>
-{{STRUCTURE_2nul|  PDB=2nul  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PPIB_ECOLI PPIB_ECOLI] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
+== 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/nu/2nul_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=2nul ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The structure of the unliganded form of the Escherichia coli cytoplasmic peptidyl-prolyl isomerase (ppiB gene product) in a new crystal form was determined by the molecular replacement method and refined to an R-factor of 16.1% at 2.1 A resolution. The enzyme crystallized in the orthorhombic C2221 space group with unit cell dimensions of a=44.7 A, b=68.2 A and c=102.0 A. Comparison with the reported structure of the enzyme complexed with the tripeptide substrate succinyl-Ala-Pro-Ala-p-nitroanilide revealed subtle changes that occur upon complex formation. There is evidence to suggest that two surface loops have significantly reduced mobility in the complexed structure.
-===PEPTIDYLPROLYL ISOMERASE FROM E. COLI===
+Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: evidence for decreased mobility of loops upon complexation.,Edwards KJ, Ollis DL, Dixon NE J Mol Biol. 1997 Aug 15;271(2):258-65. PMID:9268657<ref>PMID:9268657</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2nul" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_9268657}}, adds the Publication Abstract to the page
+*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 9268657 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9268657}}
+__TOC__
+</StructureSection>
-==About this Structure==
-NUL is a 1 chain structure of sequence 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=2NUL OCA].
-==Reference==
-<ref group="xtra">PMID:9268657</ref><references group="xtra"/>
 [[Category: Escherichia coli]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Large Structures]]
-[[Category: Edwards, K J.]]
+[[Category: Edwards KJ]]
-[[Category: Ollis, D L.]]
+[[Category: Ollis DL]]
-[[Category: Isomerase]]
-[[Category: Rotamase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 06:41:51 2009''