4r3e: Difference between revisions
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New page: '''Unreleased structure''' The entry 4r3e is ON HOLD Authors: Ulrich, A., Wahl, M.C. Description: Structure of a spliceosomal protein from Homo sapiens |
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==Structure of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27 from Homo sapiens== | |||
<StructureSection load='4r3e' size='340' side='right'caption='[[4r3e]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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='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> | |||
</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®/PubMed®, 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__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Ulrich A]] | |||
[[Category: Wahl MC]] | |||
Latest revision as of 17:43, 20 September 2023
Structure of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27 from Homo sapiens
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