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New page: left|200px<br /><applet load="2nul" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nul, resolution 2.1Å" /> '''PEPTIDYLPROLYL ISOMER...
 
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[[Image:2nul.jpg|left|200px]]<br /><applet load="2nul" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2nul, resolution 2.1&Aring;" />
'''PEPTIDYLPROLYL ISOMERASE FROM E. COLI'''<br />


==Overview==
==PEPTIDYLPROLYL ISOMERASE FROM E. COLI==
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.
<StructureSection load='2nul' size='340' side='right'caption='[[2nul]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
</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.


==About this Structure==
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>
2NUL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NUL OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9268657 9268657]
</div>
<div class="pdbe-citations 2nul" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Edwards KJ]]
[[Category: Edwards, K.J.]]
[[Category: Ollis DL]]
[[Category: Ollis, D.L.]]
[[Category: isomerase]]
[[Category: rotamase]]
 
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Latest revision as of 06:46, 9 August 2023

PEPTIDYLPROLYL ISOMERASE FROM E. COLI

2nul, resolution 2.10Å

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