5XNM
Structure of unstacked C2S2M2-type PSII-LHCII supercomplex from Pisum sativum
Summary for 5XNM
Entry DOI | 10.2210/pdb5xnm/pdb |
EMDB information | 6742 |
Descriptor | Chlorophyll a-b binding protein 8, chloroplastic, Photosystem II reaction center protein H, Photosystem II reaction center protein I, PsbI, ... (39 entities in total) |
Functional Keywords | photosystem ii, psii-lhcii, c2s2m2, supercomplex, membrane protein |
Biological source | Pisum sativum (Garden pea) More |
Total number of polymer chains | 54 |
Total formula weight | 1436522.06 |
Authors | Su, X.D.,Ma, J.,Wei, X.P.,Cao, P.,Zhu, D.J.,Chang, W.R.,Liu, Z.F.,Zhang, X.Z.,Li, M. (deposition date: 2017-05-23, release date: 2017-09-20, Last modification date: 2019-05-01) |
Primary citation | Su, X.,Ma, J.,Wei, X.,Cao, P.,Zhu, D.,Chang, W.,Liu, Z.,Zhang, X.,Li, M. Structure and assembly mechanism of plant C2S2M2-type PSII-LHCII supercomplex Science, 357:815-820, 2017 Cited by PubMed Abstract: In plants, the photosynthetic machinery photosystem II (PSII) consists of a core complex associated with variable numbers of light-harvesting complexes II (LHCIIs). The supercomplex, comprising a dimeric core and two strongly bound and two moderately bound LHCIIs (CSM), is the dominant form in plants acclimated to limited light. Here we report cryo-electron microscopy structures of two forms of CSM (termed stacked and unstacked) from at 2.7- and 3.2-angstrom resolution, respectively. In each CSM, the moderately bound LHCII assembles specifically with a peripheral antenna complex CP24-CP29 heterodimer and the strongly bound LHCII, to establish a pigment network that facilitates light harvesting at the periphery and energy transfer into the core. The high mobility of peripheral antennae, including the moderately bound LHCII and CP24, provides insights into functional regulation of plant PSII. PubMed: 28839073DOI: 10.1126/science.aan0327 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
Download full validation report