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4FBY

fs X-ray diffraction of Photosystem II

Summary for 4FBY
Entry DOI10.2210/pdb4fby/pdb
Related3BZ1 3BZ2
DescriptorPhotosystem Q(B) protein 1, Photosystem II reaction center protein K, Photosystem II reaction center protein L, ... (35 entities in total)
Functional Keywordsphotosystem, ps ii, ps2, membrane complex, transmembrane alpha-helix, photosynthesis, x-ray free electron laser, photosystem ii, reaction center, iron, manganese, light harvesting, electron transport, water oxidation, thylakoid membrane
Biological sourceThermosynechococcus elongatus
More
Cellular locationCellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379, 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 Q8CM25
Cellular thylakoid membrane ; Single-pass membrane protein : Q9F1K9 Q8DIN8 Q8DHA7 Q8DIQ0 Q8DJI1 Q9F1R6 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_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:0000255|HAMAP-Rule:MF_00643, 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 chains40
Total formula weight741329.84
Authors
Primary citationKern, J.,Alonso-Mori, R.,Hellmich, J.,Tran, R.,Hattne, J.,Laksmono, H.,Glockner, C.,Echols, N.,Sierra, R.G.,Sellberg, J.,Lassalle-Kaiser, B.,Gildea, R.J.,Glatzel, P.,Grosse-Kunstleve, R.W.,Latimer, M.J.,McQueen, T.A.,DiFiore, D.,Fry, A.R.,Messerschmidt, M.,Miahnahri, A.,Schafer, D.W.,Seibert, M.M.,Sokaras, D.,Weng, T.C.,Zwart, P.H.,White, W.E.,Adams, P.D.,Bogan, M.J.,Boutet, S.,Williams, G.J.,Messinger, J.,Sauter, N.K.,Zouni, A.,Bergmann, U.,Yano, J.,Yachandra, V.K.
Room temperature femtosecond X-ray diffraction of photosystem II microcrystals.
Proc.Natl.Acad.Sci.USA, 109:9721-9726, 2012
Cited by
PubMed Abstract: Most of the dioxygen on earth is generated by the oxidation of water by photosystem II (PS II) using light from the sun. This light-driven, four-photon reaction is catalyzed by the Mn(4)CaO(5) cluster located at the lumenal side of PS II. Various X-ray studies have been carried out at cryogenic temperatures to understand the intermediate steps involved in the water oxidation mechanism. However, the necessity for collecting data at room temperature, especially for studying the transient steps during the O-O bond formation, requires the development of new methodologies. In this paper we report room temperature X-ray diffraction data of PS II microcrystals obtained using ultrashort (< 50 fs) 9 keV X-ray pulses from a hard X-ray free electron laser, namely the Linac Coherent Light Source. The results presented here demonstrate that the "probe before destroy" approach using an X-ray free electron laser works even for the highly-sensitive Mn(4)CaO(5) cluster in PS II at room temperature. We show that these data are comparable to those obtained in synchrotron radiation studies as seen by the similarities in the overall structure of the helices, the protein subunits and the location of the various cofactors. This work is, therefore, an important step toward future studies for resolving the structure of the Mn(4)CaO(5) cluster without any damage at room temperature, and of the reaction intermediates of PS II during O-O bond formation.
PubMed: 22665786
DOI: 10.1073/pnas.1204598109
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (6.56 Å)
Structure validation

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