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5X56

Crystal structure of PSB27 from Arabidopsis thaliana

Summary for 5X56
Entry DOI10.2210/pdb5x56/pdb
DescriptorPhotosystem II repair protein PSB27-H1, chloroplastic (2 entities in total)
Functional Keywordsphotosynthesis protein, photosynthesis
Biological sourceArabidopsis thaliana (Mouse-ear cress)
Cellular locationPlastid, chloroplast thylakoid membrane ; Peripheral membrane protein ; Lumenal side : Q9LR64
Total number of polymer chains2
Total formula weight23442.57
Authors
Liu, J.,Cheng, X. (deposition date: 2017-02-15, release date: 2017-12-27, Last modification date: 2023-11-22)
Primary citationCheng, X.,Liu, J.,Huan, Z.,Fudong, L.,Shuya, Z.,Min, X.,Ke, R.,Yuhua, W.,Aigen, F.
Crystal structure of Psb27 from Arabidopsis thaliana determined at a resolution of 1.85 angstrom.
Photosyn. Res., 136:139-146, 2018
Cited by
PubMed Abstract: Proper biogenesis and maintenance of photosynthetic thylakoid membrane complexes are essential for the photosynthetic light reactions. A thylakoid lumenal protein, Psb27, plays a vital role in assembly or/and maintenance of photosystem II (PSII). In cyanobacteria, it is a small lipoprotein docked to the lumenal side of PSII, and functions in the assembly of the MnCa cluster and in the PSII repair cycle. However, Psb27 from Arabidopsis thaliana is not a lipoprotein, and it is involved in PSII repair and acclimation to fluctuating light stress, suggesting a functional divergence between Arabidopsis Psb27 and cyanobacterial Psb27s. To gain a better understanding of Psb27 from higher plants, we determined the crystal structure of Arabidopsis Psb27 by X-ray crystallography at a resolution of 1.85 Å. The structure of Arabidopsis Psb27 is a four-helix bundle, similar to its orthologues from cyanobacteria. However, there are several structural differences between Arabidopsis Psb27 and cyanobacterial Psb27s concerning the overall molecular shape, the N- and C-terminal structures, and the surface charge. These differences suggest that Psb27 from higher plants and cyanobacteria may function differently.
PubMed: 29098572
DOI: 10.1007/s11120-017-0450-3
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

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数据于2024-11-06公开中

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