6HMZ

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

Summary for 6HMZ

• Entry DOI: 10.2210/pdb6hmz/pdb
• Descriptor: Peptidyl-prolyl cis-trans isomerase, Cyclosporin, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: peptidyl-prolyl cis/trans isomerase, phloem sap, cyp-like domain, cyclophilin diversity, cyclosporin a, isomerase
• Biological source: Brassica napus (Rape); More
• Total number of polymer chains: 2
• Total formula weight: 20718.00

Authors

Falke, S.,Hanhart, P.,Garbe, M.,Thiess, M.,Betzel, C.,Kehr, J. (deposition date: 2018-09-13, release date: 2018-11-21, Last modification date: 2024-01-24)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.98 Å)