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6KAF

C2S2M2N2-type PSII-LHCII

This is a non-PDB format compatible entry.
Summary for 6KAF
Entry DOI10.2210/pdb6kaf/pdb
EMDB information9957
DescriptorChlorophyll a-b binding protein CP29, Photosystem II reaction center protein M, Oxygen-evolving enhancer protein 1 of photosystem II, ... (37 entities in total)
Functional Keywordsphotosystem ii, c2s2m2n2-type psii-lhcii, photosynthesis
Biological sourceChlamydomonas reinhardtii
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Total number of polymer chains58
Total formula weight1662088.14
Authors
Chang, S.H.,Shen, L.L.,Huang, Z.H.,Wang, W.D.,Han, G.Y.,Shen, J.R.,Zhang, X. (deposition date: 2019-06-22, release date: 2019-10-23, Last modification date: 2019-11-20)
Primary citationShen, L.,Huang, Z.,Chang, S.,Wang, W.,Wang, J.,Kuang, T.,Han, G.,Shen, J.R.,Zhang, X.
Structure of a C2S2M2N2-type PSII-LHCII supercomplex from the green algaChlamydomonas reinhardtii.
Proc.Natl.Acad.Sci.USA, 116:21246-21255, 2019
Cited by
PubMed Abstract: Photosystem II (PSII) in the thylakoid membranes of plants, algae, and cyanobacteria catalyzes light-induced oxidation of water by which light energy is converted to chemical energy and molecular oxygen is produced. In higher plants and most eukaryotic algae, the PSII core is surrounded by variable numbers of light-harvesting antenna complex II (LHCII), forming a PSII-LHCII supercomplex. In order to harvest energy efficiently at low-light-intensity conditions under water, a complete PSII-LHCII supercomplex (CSMN) of the green alga (Cr) contains more antenna subunits and pigments than the dominant PSII-LHCII supercomplex (CSM) of plants. The detailed structure and energy transfer pathway of the Cr-PSII-LHCII remain unknown. Here we report a cryoelectron microscopy structure of a complete, CSMN-type PSII-LHCII supercomplex from at 3.37-Å resolution. The results show that the Cr-CSMN supercomplex is organized as a dimer, with 3 LHCII trimers, 1 CP26, and 1 CP29 peripheral antenna subunits surrounding each PSII core. The N-LHCII trimer partially occupies the position of CP24, which is present in the higher-plant PSII-LHCII but absent in the green alga. The M trimer is rotated relative to the corresponding M trimer in plant PSII-LHCII. In addition, some unique features were found in the green algal PSII core. The arrangement of a huge number of pigments allowed us to deduce possible energy transfer pathways from the peripheral antennae to the PSII core.
PubMed: 31570614
DOI: 10.1073/pnas.1912462116
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.73 Å)
Structure validation

226707

數據於2024-10-30公開中

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