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Structure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Ulrich, Alexander Carsten Wahl, Markus C. |
| Copyright Year | 2014 |
| Abstract | 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 Å 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 Å 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. |
| Starting Page | 787 |
| Ending Page | 800 |
| Page Count | 14 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://journals.iucr.org/d/issues/2014/12/00/dw5118/dw5118sup1.pdf |
| PubMed reference number | 25478830v1 |
| Alternate Webpage(s) | https://doi.org/10.1107/S1399004714021695 |
| DOI | 10.1107/S1399004714021695 |
| Journal | Acta crystallographica. Section D, Biological crystallography |
| Volume Number | 70 |
| Part | 12 |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Appendix CWC27 gene Carcinoma in Situ Clinical act of insertion Endopeptidases Exhibits as Topic Fungi Insertion Mutation Peptidylprolyl Isomerase Proline Sequence Alignment Thioctic Acid U2-type spliceosomal complex procollagen Type I N-terminal peptide prostaglandin E synthase |
| Content Type | Text |
| Resource Type | Article |
