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4XK8

Crystal structure of plant photosystem I-LHCI super-complex at 2.8 angstrom resolution

Summary for 4XK8
Entry DOI10.2210/pdb4xk8/pdb
DescriptorPhotosystem I P700 chlorophyll a apoprotein A1, Photosystem I reaction center subunit IX, Photosystem I reaction center subunit X psaK, ... (29 entities in total)
Functional Keywordsphotosynthesis, photosystem i, plant lhci-psi supercomplex
Biological sourcePisum sativum (Garden pea)
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Total number of polymer chains32
Total formula weight1046378.51
Authors
Suga, M.,Qin, X.,Kuang, T.,Shen, J.R. (deposition date: 2015-01-10, release date: 2015-06-10, Last modification date: 2024-11-20)
Primary citationQin, X.,Suga, M.,Kuang, T.,Shen, J.R.
Structural basis for energy transfer pathways in the plant PSI-LHCI supercomplex
Science, 348:989-995, 2015
Cited by
PubMed Abstract: Photosynthesis converts solar energy to chemical energy by means of two large pigment-protein complexes: photosystem I (PSI) and photosystem II (PSII). In higher plants, the PSI core is surrounded by a large light-harvesting complex I (LHCI) that captures sunlight and transfers the excitation energy to the core with extremely high efficiency. We report the structure of PSI-LHCI, a 600-kilodalton membrane protein supercomplex, from Pisum sativum (pea) at a resolution of 2.8 angstroms. The structure reveals the detailed arrangement of pigments and other cofactors—especially within LHCI—as well as numerous specific interactions between the PSI core and LHCI. These results provide a firm structural basis for our understanding on the energy transfer and photoprotection mechanisms within the PSI-LHCI supercomplex.
PubMed: 26023133
DOI: 10.1126/science.aab0214
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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