6yp7

PSII-LHCII C2S2 supercomplex from Pisum sativum grown in high light conditions

spinqualitylabelsall models 6yp7, resolution 3.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6yp7 is a 24 chain structure with sequence from Pisum sativum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.8Å Ligands: BCR, BCT, CL, CLA, DGD, FE2, HEM, LHG, LMG, LUT, NEX, PHO, PL9, SQD, XAT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CB28_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. May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen. Publication Abstract from PubMed In 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Photosystem II 3D structures

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