6LXO

TvCyP2 in apo form 1

6LXO の概要

• エントリーDOI: 10.2210/pdb6lxo/pdb
• 分子名称: Peptidyl-prolyl cis-trans isomerase, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: peptidyl -prolyl isomerase, self association, cytosolic protein, isomerase
• 由来する生物種: Trichomonas vaginalis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21738.63

構造登録者

Aryal, S.,Chen, C.,Hsu, C.H. (登録日: 2020-02-11, 公開日: 2020-09-09, 最終更新日: 2023-11-29)

主引用文献

Aryal, S.,Hsu, H.M.,Lou, Y.C.,Chu, C.H.,Tai, J.H.,Hsu, C.H.,Chen, C.
N-Terminal Segment of TvCyP2 Cyclophilin fromTrichomonas vaginalisIs Involved in Self-Association, Membrane Interaction, and Subcellular Localization.
Biomolecules, 10:-, 2020

PubMed Abstract: In (), cyclophilins play a vital role in dislodging Myb proteins from the membrane compartment and leading them to nuclear translocation. We previously reported that CyP1 cyclophilin from forms a dimer and plays an essential role in moving the Myb1 transcription factor toward the nucleus. In comparison, CyP2 containing an extended segment at the N-terminus (N-terminal segment) formed a monomer and showed a different role in regulating protein trafficking. Four X-ray structures of CyP2 were determined under various conditions, all showing the N-terminal segment interacting with the active site of a neighboring CyP2, an unusual interaction. NMR study revealed that this particular interaction exists in solution as well and also the N-terminal segment seems to interact with the membrane. In vivo study of CyP2 and CyP2-∆N (CyP2 without the N-terminal segment) indicated that both proteins have different subcellular localization. Together, the structural and functional characteristics at the N-terminal segment offer valuable information for insights into the mechanism of how CyP2 regulates protein trafficking, which may be applied in drug development to prevent pathogenesis and disease progression in infection.

PubMed: 32859063
DOI: 10.3390/biom10091239

実験手法

X-RAY DIFFRACTION (1.89 Å)