Enzyme Activity and Structural Features of Three Single-domain Phloem Cyclophilins from Brassica Napus

Overview

Journal Sci Rep

Specialty Science

Date 2019 Jun 29

PMID 31249367

Citations 4

Authors

Patrizia Hanhart

Sven Falke

Marcel Garbe

Victoria Rose

Melanie Thiess

Christian Betzel

Julia Kehr

Affiliations

Soon will be listed here.

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.

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