7D0J
Photosystem I-LHCI-LHCII of Chlamydomonas reinhardtii
Summary for 7D0J
Entry DOI | 10.2210/pdb7d0j/pdb |
EMDB information | 30536 |
Descriptor | Photosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit IX, Photosystem I reaction center subunit psaK, chloroplastic, ... (36 entities in total) |
Functional Keywords | psi-lhci-lhcii, photosynthesis |
Biological source | Chlamydomonas reinhardtii (Chlamydomonas smithii) More |
Total number of polymer chains | 29 |
Total formula weight | 1016082.76 |
Authors | Wang, W.D.,Shen, L.L.,Huang, Z.H.,Han, G.Y.,Zhang, X.,Shen, J.R. (deposition date: 2020-09-10, release date: 2021-03-03, Last modification date: 2024-10-23) |
Primary citation | Huang, Z.,Shen, L.,Wang, W.,Mao, Z.,Yi, X.,Kuang, T.,Shen, J.R.,Zhang, X.,Han, G. Structure of photosystem I-LHCI-LHCII from the green alga Chlamydomonas reinhardtii in State 2. Nat Commun, 12:1100-1100, 2021 Cited by PubMed Abstract: Photosystem I (PSI) and II (PSII) balance their light energy distribution absorbed by their light-harvesting complexes (LHCs) through state transition to maintain the maximum photosynthetic performance and to avoid photodamage. In state 2, a part of LHCII moves to PSI, forming a PSI-LHCI-LHCII supercomplex. The green alga Chlamydomonas reinhardtii exhibits state transition to a far larger extent than higher plants. Here we report the cryo-electron microscopy structure of a PSI-LHCI-LHCII supercomplex in state 2 from C. reinhardtii at 3.42 Å resolution. The result reveals that the PSI-LHCI-LHCII of C. reinhardtii binds two LHCII trimers in addition to ten LHCI subunits. The PSI core subunits PsaO and PsaH, which were missed or not well-resolved in previous Cr-PSI-LHCI structures, are observed. The present results reveal the organization and assembly of PSI core subunits, LHCI and LHCII, pigment arrangement, and possible pathways of energy transfer from peripheral antennae to the PSI core. PubMed: 33597543DOI: 10.1038/s41467-021-21362-6 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.42 Å) |
Structure validation
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