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Structural Insights into a Dimeric Psb27-photosystem II Complex from a Cyanobacterium

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Specialty Science
Date 2021 Jan 26
PMID 33495333
Citations 31
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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.

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References
1.
Liu H, Huang R, Chen J, Gross M, Pakrasi H . Psb27, a transiently associated protein, binds to the chlorophyll binding protein CP43 in photosystem II assembly intermediates. Proc Natl Acad Sci U S A. 2011; 108(45):18536-41. PMC: 3215006. DOI: 10.1073/pnas.1111597108. View

2.
Mabbitt P, Rautureau G, Day C, Wilbanks S, Eaton-Rye J, Hinds M . Solution structure of Psb27 from cyanobacterial photosystem II. Biochemistry. 2009; 48(37):8771-3. DOI: 10.1021/bi901309c. View

3.
Roose J, Kashino Y, Pakrasi H . The PsbQ protein defines cyanobacterial Photosystem II complexes with highest activity and stability. Proc Natl Acad Sci U S A. 2007; 104(7):2548-53. PMC: 1892988. DOI: 10.1073/pnas.0609337104. View

4.
Nowaczyk M, Krause K, Mieseler M, Sczibilanski A, Ikeuchi M, Rogner M . Deletion of psbJ leads to accumulation of Psb27-Psb28 photosystem II complexes in Thermosynechococcus elongatus. Biochim Biophys Acta. 2012; 1817(8):1339-45. DOI: 10.1016/j.bbabio.2012.02.017. View

5.
Xiao Y, Zhu Q, Yang Y, Wang W, Kuang T, Shen J . Role of PsbV-Tyr137 in photosystem II studied by site-directed mutagenesis in the thermophilic cyanobacterium Thermosynechococcus vulcanus. Photosynth Res. 2020; 146(1-3):41-54. DOI: 10.1007/s11120-020-00753-8. View