Enzyme activity and structural features of three single-domain phloem cyclophilins from Brassica napus.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
27 06 2019
27 06 2019
Historique:
received:
20
09
2018
accepted:
14
06
2019
entrez:
29
6
2019
pubmed:
30
6
2019
medline:
24
10
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 31249367
doi: 10.1038/s41598-019-45856-y
pii: 10.1038/s41598-019-45856-y
pmc: PMC6597583
doi:
Substances chimiques
Cyclophilins
EC 5.2.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
9368Références
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