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| | <StructureSection load='4r3e' size='340' side='right'caption='[[4r3e]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='4r3e' size='340' side='right'caption='[[4r3e]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4r3e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hq6|2hq6]], [[4r3f|4r3f]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CWC27, SDCCAG10, UNQ438/PRO871 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[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://pdbe.org/4r3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r3e RCSB], [http://www.ebi.ac.uk/pdbsum/4r3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r3e ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CWC27_HUMAN CWC27_HUMAN]] PPIases accelerate the folding of proteins. | + | [https://www.uniprot.org/uniprot/CWC27_HUMAN CWC27_HUMAN] PPIases accelerate the folding of proteins. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peptidylprolyl isomerase]]
| + | [[Category: Ulrich A]] |
| - | [[Category: Ulrich, A]] | + | [[Category: Wahl MC]] |
| - | [[Category: Wahl, M C]] | + | |
| - | [[Category: Cyclophilin-type ppiase]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| Structural highlights
Function
CWC27_HUMAN PPIases accelerate the folding of proteins.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ulrich A, Wahl MC. Structure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27. Acta Crystallogr D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3110-23. doi:, 10.1107/S1399004714021695. Epub 2014 Nov 22. PMID:25478830 doi:http://dx.doi.org/10.1107/S1399004714021695
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