TY - JOUR
T1 - Structural insights into cyanobacterial photosystem II intermediates associated with Psb28 and Tsl0063
AU - Xiao, Yanan
AU - Huang, Guoqiang
AU - You, Xin
AU - Zhu, Qingjun
AU - Wang, Wenda
AU - Kuang, Tingyun
AU - Han, Guangye
AU - Sui, Sen Fang
AU - Shen, Jian Ren
N1 - Funding Information:
We thank J. Lei and the staff at the Tsinghua University Branch of the National Center for Protein Sciences Beijing for providing facility support, the Explorer 100 cluster system of the Tsinghua National Laboratory for Information Science and Technology for providing computation resources, and H. Deng and X. Meng in the Proteinomics Facility at the Technology Center for Protein Sciences, Tsinghua University, for protein MS analysis. This work was supported by the National Key R&D Program of China (grant nos. 2017YFA0503700, 2016YFA0501101, 2017YFA0504600, 2020YFA0907600 and 2019YFA0906300), the National Natural Science Foundation of China (grant no. 31470339), the Strategic Priority Research Program of CAS (grant nos. XDA27050402 and XDB17000000), a CAS Key Research programme for Frontier Science (grant no. QYZDY-SSW-SMC003), Youth Innovation Promotion Association of CAS (grant no. 2020081) and CAS Interdisciplinary Innovation Team (grant no. JCTD-2020-06).
Publisher Copyright:
© 2021, The Author(s), under exclusive licence to Springer Nature Limited.
PY - 2021/8
Y1 - 2021/8
N2 - Photosystem II (PSII) is a multisubunit pigment–protein complex and catalyses light-induced water oxidation, leading to the conversion of light energy into chemical energy and the release of dioxygen. We analysed the structures of two Psb28-bound PSII intermediates, Psb28–RC47 and Psb28–PSII, purified from a psbV-deletion strain of the thermophilic cyanobacterium Thermosynechococcus vulcanus, using cryo-electron microscopy. Both Psb28–RC47 and Psb28–PSII bind one Psb28, one Tsl0063 and an unknown subunit. Psb28 is located at the cytoplasmic surface of PSII and interacts with D1, D2 and CP47, whereas Tsl0063 is a transmembrane subunit and binds at the side of CP47/PsbH. Substantial structural perturbations are observed at the acceptor side, which result in conformational changes of the quinone (QB) and non-haem iron binding sites and thus may protect PSII from photodamage during assembly. These results provide a solid structural basis for understanding the assembly process of native PSII.
AB - Photosystem II (PSII) is a multisubunit pigment–protein complex and catalyses light-induced water oxidation, leading to the conversion of light energy into chemical energy and the release of dioxygen. We analysed the structures of two Psb28-bound PSII intermediates, Psb28–RC47 and Psb28–PSII, purified from a psbV-deletion strain of the thermophilic cyanobacterium Thermosynechococcus vulcanus, using cryo-electron microscopy. Both Psb28–RC47 and Psb28–PSII bind one Psb28, one Tsl0063 and an unknown subunit. Psb28 is located at the cytoplasmic surface of PSII and interacts with D1, D2 and CP47, whereas Tsl0063 is a transmembrane subunit and binds at the side of CP47/PsbH. Substantial structural perturbations are observed at the acceptor side, which result in conformational changes of the quinone (QB) and non-haem iron binding sites and thus may protect PSII from photodamage during assembly. These results provide a solid structural basis for understanding the assembly process of native PSII.
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U2 - 10.1038/s41477-021-00961-7
DO - 10.1038/s41477-021-00961-7
M3 - Article
C2 - 34226692
AN - SCOPUS:85109673404
SN - 2055-026X
VL - 7
SP - 1132
EP - 1142
JO - Nature Plants
JF - Nature Plants
IS - 8
ER -