4v62

Crystal Structure of cyanobacterial Photosystem II

spinqualitylabelsall models 4v62, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4v62 is a 40 chain structure with sequence from Thermosynechococcus elongatus. This structure supersedes the now removed PDB entries and 3bz2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BCR, BCT, CA, CL, CLA, DGD, FE2, HEM, LHG, LMG, LMT, OEC, PHO, PL9, SQD NonStd Res: UNK Related: 3bz1, 3bz2 Resources: FirstGlance, OCA, RCSB, PDBsum Function [PSBL_THEEB] Required for PSII activity (By similarity). [PSBB_THEEB] One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01495] [YCF12_THEEB] A core subunit of photosystem II (PSII).[HAMAP-Rule:MF_01329] [PSBA1_SYNEL] This is one of the two reaction center proteins of photosystem II (By similarity). [CY550_THEEB] Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II. It is not essential for growth under normal conditions but is required under low CO(2) concentrations.[HAMAP-Rule:MF_01378] [PSBF_THEEB] This b-type cytochrome is tightly associated with the reaction center of photosystem II and possibly is part of the water-oxidation complex (By similarity).[HAMAP-Rule:MF_00643] [PSBC_THEEB] One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01496] [PSBJ_THEEB] This protein is a component of the reaction center of photosystem II (By similarity). [PSBT_THEEB] Seems to play a role in the dimerization of PSII. [PSBU_THEEB] Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation (By similarity).[HAMAP-Rule:MF_00589] [PSBZ_THEEB] Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. May also aid in binding of PsbK, Ycf12 and the oxygen-evolving complex to PSII, at least in vitro. [PSBI_THEEB] This protein is a component of the reaction center of photosystem II.[HAMAP-Rule:MF_01316] [PSBK_THEEB] This protein is a component of the reaction center of photosystem II.[HAMAP-Rule:MF_00441] [PSBE_THEEB] This b-type cytochrome is tightly associated with the reaction center of photosystem II and possibly is part of the water-oxidation complex.[HAMAP-Rule:MF_00642] Publication Abstract from PubMed Photosystem II (PSII) is a large homodimeric protein-cofactor complex located in the photosynthetic thylakoid membrane that acts as light-driven water:plastoquinone oxidoreductase. The crystal structure of PSII from Thermosynechococcus elongatus at 2.9-A resolution allowed the unambiguous assignment of all 20 protein subunits and complete modeling of all 35 chlorophyll a molecules and 12 carotenoid molecules, 25 integral lipids and 1 chloride ion per monomer. The presence of a third plastoquinone Q(C) and a second plastoquinone-transfer channel, which were not observed before, suggests mechanisms for plastoquinol-plastoquinone exchange, and we calculated other possible water or dioxygen and proton channels. Putative oxygen positions obtained from a Xenon derivative indicate a role for lipids in oxygen diffusion to the cytoplasmic side of PSII. The chloride position suggests a role in proton-transfer reactions because it is bound through a putative water molecule to the Mn(4)Ca cluster at a distance of 6.5 A and is close to two possible proton channels. Cyanobacterial photosystem II at 2.9-A resolution and the role of quinones, lipids, channels and chloride.,Guskov A, Kern J, Gabdulkhakov A, Broser M, Zouni A, Saenger W Nat Struct Mol Biol. 2009 Mar;16(3):334-42. Epub 2009 Feb 15. PMID:19219048 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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