21wv | pdb_000021wv

In situ structure of the C2S2M2L4-type PSII-LHCII supercomplex from Oryza sativa

spinqualitylabelsall models 21wv, resolution 2.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 21wv is a 36 chain structure with sequence from Oryza sativa Japonica Group. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.89Å Ligands: 3PH, BCR, BCT, CL, CLA, DGD, FE2, HEM, LHG, LNL, LUT, MGE, OEX, PHO, PL9, SQD, VIV, XAT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CB22_ORYSJ The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. Publication Abstract from PubMed Photosynthesis sustains life on Earth by converting light to chemical energy through the coordinated action of photosystem I (PSI) and photosystem II (PSII) within thylakoid membranes(1-4). Although structures of isolated photosystems are available, their native organization in chloroplasts remains unknown. Here, using in situ cryo-electron microscopy, we directly imaged Oryza sativa (rice) chloroplasts and determined structures of photosystem supercomplexes in their native membrane environment. We resolved a C(2)S(2)M(2)L(4)-type PSII-light harvesting complex II (LHCII) supercomplex, including four LHCII antenna trimers that were not retained in purified preparations. Excitation energy transfer calculations based on this architecture closely reproduce in vivo measurements, indicating its physiological relevance. We also resolved asymmetric PSII-LHCII dimers, including side-by-side, trans-lumenal and trans-stromal architectures, and higher-order assemblies of trimers and tetramers. On the basis of these observations, we propose that PSII forms a trans-lumenal and trans-stromal 'skeleton' that shapes thylakoid morphology and supports grana stacking. In addition, we obtained high-resolution structures of PSI-LHCI-LHCII and PSI-LHCI supercomplexes. Together, these structures reveal extensive networks of lipids, pigments and cofactors, providing the first molecular framework for understanding how the native architecture of plant photosystem supports the exceptional photon-to-electron efficiency of photosynthesis. In situ structures of plant photosystem supercomplexes.,Li J, Elias E, Zhang K, Croce R, Zhu J Nature. 2026 Jul 29. doi: 10.1038/s41586-026-10847-3. PMID:42527593 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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