9LH4
Crystal structure of the cyclophilin 37 from Arabidopsis thaliana
Summary for 9LH4
| Entry DOI | 10.2210/pdb9lh4/pdb |
| Descriptor | Peptidyl-prolyl cis-trans isomerase CYP37, chloroplastic (2 entities in total) |
| Functional Keywords | arabidopsis thaliana, cyp37, plant protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 41437.73 |
| Authors | |
| Primary citation | Han, X.,Jiang, J.,Lu, Z.,Bai, J.,Qin, X.,Dong, S. Crystal structure of cyclophilin 37 from Arabidopsis thaliana. Acta Crystallogr.,Sect.F, 81:171-176, 2025 Cited by PubMed Abstract: Photosynthesis is the largest-scale energy and material conversion process on Earth. The cytchrome (Cyt) bf complex plays a crucial role in photosynthesis. Under high-light conditions, cyclophilin 37 (CYP37) in Arabidopsis thaliana (AtCYP37) can interact with the PetA subunit of Cyt bf, thereby helping plants initiate photoprotection. Here, we purified, crystallized and determined a 1.95 Å resolution structure of AtCYP37. Overall, AtCYP37 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 AtCYP37 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. PubMed: 40091855DOI: 10.1107/S2053230X25001979 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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