6HMZ

Crystal Structure of a Single-Domain Cyclophilin from Brassica napus Phloem Sap

6HMZ の概要

• エントリーDOI: 10.2210/pdb6hmz/pdb
• 分子名称: Peptidyl-prolyl cis-trans isomerase, Cyclosporin, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: peptidyl-prolyl cis/trans isomerase, phloem sap, cyp-like domain, cyclophilin diversity, cyclosporin a, isomerase
• 由来する生物種: Brassica napus (Rape); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20718.00

構造登録者

Falke, S.,Hanhart, P.,Garbe, M.,Thiess, M.,Betzel, C.,Kehr, J. (登録日: 2018-09-13, 公開日: 2018-11-21, 最終更新日: 2024-01-24)

主引用文献

Hanhart, P.,Falke, S.,Garbe, M.,Rose, V.,Thiess, M.,Betzel, C.,Kehr, J.
Enzyme activity and structural features of three single-domain phloem cyclophilins from Brassica napus.
Sci Rep, 9:9368-9368, 2019

PubMed Abstract: Cyclophilins (CYPs) are a group of ubiquitous prolyl cis/trans isomerases (PPIases). It was shown that plants possess the most diverse CYP families and that these are abundant in the phloem long-distance translocation stream. Since phloem exudate showed PPIase activity, three single-domain CYPs that occur in phloem samples from Brassica napus were characterised on functional and structural levels. It could be shown that they exhibit isomerase activity and that this activity is controlled by a redox regulation mechanism, which has been postulated for divergent CYPs. The structure determination by small-angle X-ray scattering experiments revealed a conserved globular shape. In addition, the high-resolution crystal structure of BnCYP19-1 was resolved and refined to 2.0 Å resolution, and the active sites of related CYPs as well as substrate binding were modelled. The obtained data and results support the hypothesis that single domain phloem CYPs are active phloem PPIases that may function as chaperones.

PubMed: 31249367
DOI: 10.1038/s41598-019-45856-y

実験手法

X-RAY DIFFRACTION (1.98 Å)