6yp7 | pdb_00006yp7
PSII-LHCII C2S2 supercomplex from Pisum sativum grown in high light conditions
Structural highlights
FunctionCB28_PEA The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.[1] May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.[2] Publication Abstract from PubMedIn plant grana thylakoid membranes Photosystem II (PSII) associates with a variable number of antenna proteins (LHCII) to form different types of supercomplexes (PSII-LHCII), whose organization is dynamically adjusted in response to light cues, with the C(2)S(2) more abundant in high-light and the C(2)S(2)M(2) in low-light. Paired PSII-LHCII supercomplexes interacting at their stromal surface from adjacent thylakoid membranes were previously suggested to mediate grana stacking. Here, we present the cryo-electron microscopy maps of paired C(2)S(2) and C(2)S(2)M(2) supercomplexes isolated from pea plants grown in high-light and low-light, respectively. These maps show a different rotational offset between the two supercomplexes in the pair, responsible for modifying their reciprocal interaction and energetic connectivity. This evidence reveals a different way by which paired PSII-LHCII supercomplexes can mediate grana stacking at diverse irradiances. Electrostatic stromal interactions between LHCII trimers almost completely overlapping in the paired C(2)S(2) can be the main determinant by which PSII-LHCII supercomplexes mediate grana stacking in plants grown in high-light, whereas the mutual interaction of stromal N-terminal loops of two facing Lhcb4 subunits in the paired C(2)S(2)M(2) can fulfil this task in plants grown in low-light. The high-light induced accumulation of the Lhcb4.3 protein in PSII-LHCII supercomplexes has been previously reported. Our cryo-electron microscopy map at 3.8 A resolution of the C(2)S(2) supercomplex isolated from plants grown in high-light suggests the presence of the Lhcb4.3 protein revealing peculiar structural features of this high-light-specific antenna important for photoprotection. High-Light versus Low-Light: Effects on Paired Photosystem II Supercomplex Structural Rearrangement in Pea Plants.,Grinzato A, Albanese P, Marotta R, Swuec P, Saracco G, Bolognesi M, Zanotti G, Pagliano C Int J Mol Sci. 2020 Nov 16;21(22):8643. doi: 10.3390/ijms21228643. PMID:33207833[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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