4xk8 | pdb_00004xk8

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

spinqualitylabelsall models 4xk8, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4xk8 is a 32 chain structure with sequence from Arabidopsis thaliana, Glycine max, Phaseolus vulgaris, Pisum sativum and Spinacia oleracea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BCR, CHL, CLA, DGD, HTG, LHG, LMG, LMT, LUT, PQN, SF4, XAT Activity: Photosystem I, with EC number 1.97.1.12 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PSAC_PEA] Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn (By similarity).[HAMAP-Rule:MF_01303] [PSAI_PEA] May help in the organization of the PsaL subunit. [CB23_PEA] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen. [PSAJ_PHAVU] May help in the organization of the PsaE and PsaF subunits. Publication Abstract from PubMed 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. Photosynthesis. Structural basis for energy transfer pathways in the plant PSI-LHCI supercomplex.,Qin X, Suga M, Kuang T, Shen JR Science. 2015 May 29;348(6238):989-95. doi: 10.1126/science.aab0214. PMID:26023133 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Photosystem I

Proteopedia Page Contributors and Editors (what is this?)

OCA