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Crystal structure of cyclophilin 37 from Arabidopsis thaliana

2025/03/14 by Xing Han, Junce Jiang, Zuokun Lu +3 · 1 voice
Biochemistry, Genetics and Molecular Biology · Immunology and Microbiology · Medicine · #Signaling Pathways in Disease #Toxin Mechanisms and Immunotoxins #PARP inhibition in cancer therapy

paper · doi:10.1107/s2053230x25001979

openalex publication_date 2025/03/14 · openalex created_date 2025/03/19 · openalex updated_date 2026/06/16

Abstract

Photosynthesis is the largest-scale energy and material conversion process on Earth. The cytchrome (Cyt) b 6 f complex plays a crucial role in photosynthesis. Under high-light conditions, cyclophilin 37 (CYP37) in Arabidopsis thaliana ( At CYP37) can interact with the PetA subunit of Cyt b 6 f , thereby helping plants initiate photoprotection. Here, we purified, crystallized and determined a 1.95 Å resolution structure of At CYP37. Overall, At CYP37 consists of an N-terminal domain dominated by α-helices and a C-terminal domain mainly composed of β-strands and random coils. The structure shows significant similarity to those of Anabaena sp. CYPA and A. thaliana CYP38. Understanding the structure of At CYP37 is significant as it may help to decipher how plants regulate photosynthesis and protect against high light damage, contributing to a broader understanding of plant photobiology and potentially guiding future research in improving plant stress tolerance.

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