4R3F

Structure of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27 from Chaetomium thermophilum

4R3F の概要

• エントリーDOI: 10.2210/pdb4r3f/pdb
• 関連するPDBエントリー: 2HQ6 4R3E
• 分子名称: spliceosomal protein CWC27, 1,2-ETHANEDIOL, 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL, ... (5 entities in total)
• 機能のキーワード: cyclophilin-type ppiase, nucleus, isomerase
• 由来する生物種: Chaetomium thermophilum var. thermophilum DSM 1495
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23416.20

構造登録者

Ulrich, A.,Wahl, M.C. (登録日: 2014-08-15, 公開日: 2014-11-19, 最終更新日: 2023-09-20)

主引用文献

Ulrich, A.,Wahl, M.C.
Structure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27.
Acta Crystallogr.,Sect.D, 70:3110-3123, 2014

PubMed 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.

PubMed: 25478830
DOI: 10.1107/S1399004714021695

実験手法

X-RAY DIFFRACTION (1.3 Å)