7CZL

Structural insights into a dimeric Psb27-photosystem II complex from a cyanobacterium Thermosynechococcus vulcanus

Summary for 7CZL

• Entry DOI: 10.2210/pdb7czl/pdb
• EMDB information: 30511
• Descriptor: Photosystem II protein D1, Photosystem II reaction center protein L, Photosystem II reaction center protein M, ... (30 entities in total)
• Functional Keywords: dimeric photosystem ii (psii)-psb27 complex from a cyanobacterium thermosynechococcus vulcanus, plant protein
• Biological source: Thermosynechococcus vulcanus; More
• Total number of polymer chains: 32
• Total formula weight: 593694.68

Authors

Pi, X.,Huang, G.,Xiao, Y. (deposition date: 2020-09-09, release date: 2021-01-20, Last modification date: 2021-02-10)

Primary citation

Huang, G.,Xiao, Y.,Pi, X.,Zhao, L.,Zhu, Q.,Wang, W.,Kuang, T.,Han, G.,Sui, S.F.,Shen, J.R.
Structural insights into a dimeric Psb27-photosystem II complex from a cyanobacterium Thermosynechococcus vulcanus .
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: Photosystem II (PSII) is a multisubunit pigment-protein complex and catalyzes light-driven water oxidation, leading to the conversion of light energy into chemical energy and the release of molecular oxygen. Psb27 is a small thylakoid lumen-localized protein known to serve as an assembly factor for the biogenesis and repair of the PSII complex. The exact location and binding fashion of Psb27 in the intermediate PSII remain elusive. Here, we report the structure of a dimeric Psb27-PSII complex purified from a deletion mutant (ΔPsbV) of the cyanobacterium , solved by cryo-electron microscopy. Our structure showed that Psb27 is associated with CP43 at the luminal side, with specific interactions formed between Helix 2 and Helix 3 of Psb27 and a loop region between Helix 3 and Helix 4 of CP43 (loop C) as well as the large, lumen-exposed and hydrophilic E-loop of CP43. The binding of Psb27 imposes some conflicts with the N-terminal region of PsbO and also induces some conformational changes in CP43, CP47, and D2. This makes PsbO unable to bind in the Psb27-PSII. Conformational changes also occurred in D1, PsbE, PsbF, and PsbZ; this, together with the conformational changes occurred in CP43, CP47, and D2, may prevent the binding of PsbU and induce dissociation of PsbJ. This structural information provides important insights into the regulation mechanism of Psb27 in the biogenesis and repair of PSII.

PubMed: 33495333
DOI: 10.1073/pnas.2018053118

Experimental method

ELECTRON MICROSCOPY (3.78 Å)