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==Structure of a spliceosomal protein from Homo sapiens==
 
<StructureSection load='4r3e' size='340' side='right' caption='[[4r3e]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
==Structure of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27 from Homo sapiens==
<StructureSection load='4r3e' size='340' side='right'caption='[[4r3e]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4r3e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R3E FirstGlance]. <br>
<table><tr><td colspan='2'>[[4r3e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R3E FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</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&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hq6|2hq6]], [[4r3f|4r3f]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=4r3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r3e OCA], [https://pdbe.org/4r3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r3e RCSB], [https://www.ebi.ac.uk/pdbsum/4r3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r3e ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r3e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r3e RCSB], [http://www.ebi.ac.uk/pdbsum/4r3e PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CWC27_HUMAN CWC27_HUMAN] PPIases accelerate the folding of proteins.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cwc27 is a spliceosomal cyclophilin-type peptidyl-prolyl cis-trans isomerase (PPIase). Here, the crystal structure of a relatively protease-resistant N-terminal fragment of human Cwc27 containing the PPIase domain was determined at 2.0 A resolution. The fragment exhibits a C-terminal appendix and resides in a reduced state compared with the previous oxidized structure of a similar fragment. By combining multiple sequence alignments spanning the eukaryotic tree of life and secondary-structure prediction, Cwc27 proteins across the entire eukaryotic kingdom were identified. This analysis revealed the specific loss of a crucial active-site residue in higher eukaryotic Cwc27 proteins, suggesting that the protein evolved from a prolyl isomerase to a pure proline binder. Noting a fungus-specific insertion in the PPIase domain, the 1.3 A resolution crystal structure of the PPIase domain of Cwc27 from Chaetomium thermophilum was also determined. Although structurally highly similar in the core domain, the C. thermophilum protein displayed a higher thermal stability than its human counterpart, presumably owing to the combined effect of several amino-acid exchanges that reduce the number of long side chains with strained conformations and create new intramolecular interactions, in particular increased hydrogen-bond networks.
Structure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27.,Ulrich A, Wahl MC Acta Crystallogr D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3110-23. doi:, 10.1107/S1399004714021695. Epub 2014 Nov 22. PMID:25478830<ref>PMID:25478830</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4r3e" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Peptidylprolyl isomerase]]
[[Category: Homo sapiens]]
[[Category: Ulrich, A]]
[[Category: Large Structures]]
[[Category: Wahl, M C]]
[[Category: Ulrich A]]
[[Category: Cyclophilin-type ppiase]]
[[Category: Wahl MC]]
[[Category: Isomerase]]
[[Category: Nucleus]]
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