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5XNM

Structure of unstacked C2S2M2-type PSII-LHCII supercomplex from Pisum sativum

Summary for 5XNM
Entry DOI10.2210/pdb5xnm/pdb
EMDB information6742
DescriptorChlorophyll a-b binding protein 8, chloroplastic, Photosystem II reaction center protein H, Photosystem II reaction center protein I, PsbI, ... (39 entities in total)
Functional Keywordsphotosystem ii, psii-lhcii, c2s2m2, supercomplex, membrane protein
Biological sourcePisum sativum (Garden pea)
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Total number of polymer chains54
Total formula weight1436522.06
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 citationSu, 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: 28839073
DOI: 10.1126/science.aan0327
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

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数据于2024-10-30公开中

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