4V62

Crystal Structure of cyanobacterial Photosystem II

This is a non-PDB format compatible entry.

Summary for 4V62

• Entry DOI: 10.2210/pdb4v62/pdb
• Related: 3BZ2
• Descriptor: Photosystem Q(B) protein, Photosystem II reaction center protein K, Photosystem II reaction center protein L, ... (35 entities in total)
• Functional Keywords: electron transport photosystem, ps ii, ps2, membrane complex, transmembrane alpha-helix, herbicide resistance, iron, metal-binding, photosynthesis, photosystem ii, thylakoid, heme, reaction center, manganese, electron transport
• Biological source: Thermosynechococcus elongatus; More
• Cellular location: Cellular thylakoid membrane {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005, ECO:0000269|Ref: P0A444 Q8DIQ1 Q8DIF8; Cellular thylakoid membrane ; Single-pass membrane protein : Q9F1K9 Q8DIN8 Q8DHA7 Q8DIQ0 Q8DJI1 Q8DJ43 Q8DJZ6 P59087; Cellular thylakoid membrane ; Peripheral membrane protein ; Lumenal side : P0A431 Q9F1L5; Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:12881497, ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005, ECO:0000269|Ref: P0A386; Cellular thylakoid membrane ; Multi- pass membrane protein : Q8DHJ2; Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005, ECO:0000269|Ref: Q8CM25; Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16049768, ECO:0000269|PubMed:16172937, ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005, ECO:0000269|Ref: Q8DIP0; Cellular thylakoid membrane {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005, ECO:0000269|Ref: Q8DIN9
• Total number of polymer chains: 40
• Total formula weight: 747447.44

Authors

Guskov, A.,Gabdulkhakov, A.,Kern, J.,Broser, M.,Zouni, A.,Saenger, W. (deposition date: 2008-01-17, release date: 2014-07-09, Last modification date: 2024-10-30)

Primary citation

Guskov, A.,Kern, J.,Gabdulkhakov, A.,Broser, M.,Zouni, A.,Saenger, W.
Cyanobacterial photosystem II at 2.9-A resolution and the role of quinones, lipids, channels and chloride
Nat.Struct.Mol.Biol., 16:334-342, 2009

PubMed Abstract: 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.

PubMed: 19219048
DOI: 10.1038/nsmb.1559

Experimental method

X-RAY DIFFRACTION (2.9 Å)