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4PJ0

Structure of T.elongatus Photosystem II, rows of dimers crystal packing

Summary for 4PJ0
Entry DOI10.2210/pdb4pj0/pdb
DescriptorPhotosystem Q(B) protein 1, Photosystem II reaction center protein K, Photosystem II reaction center protein L, ... (37 entities in total)
Functional Keywordsmembrane protein, photosystem ii, c12e8, oxidoreductase, electron transport
Biological sourceThermosynechococcus elongatus
More
Cellular locationCellular 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
Cellular thylakoid membrane ; Single-pass membrane protein : Q9F1K9 Q8DIN8 Q8DHA7 Q8DIQ0 Q8DJI1 Q9F1R6 Q8DKM3 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_01496, 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: Q8DIF8 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 chains40
Total formula weight747422.82
Authors
Hellmich, J.,Bommer, M.,Burkhardt, A.,Ibrahim, M.,Kern, J.,Meents, A.,Mueh, F.,Dobbek, H.,Zouni, A. (deposition date: 2014-05-10, release date: 2014-10-22, Last modification date: 2024-10-23)
Primary citationHellmich, J.,Bommer, M.,Burkhardt, A.,Ibrahim, M.,Kern, J.,Meents, A.,Muh, F.,Dobbek, H.,Zouni, A.
Native-like Photosystem II Superstructure at 2.44 angstrom Resolution through Detergent Extraction from the Protein Crystal.
Structure, 22:1607-1615, 2014
Cited by
PubMed Abstract: Photosystem II (PSII) catalyzes a key step in photosynthesis, the oxidation of water to oxygen. Excellent structural models exist for the dimeric PSII core complex of cyanobacteria, but higher order physiological assemblies readily dissociate when solubilized from the native thylakoid membrane with detergent. Here, we describe the crystallization of PSII from Thermosynechococcus elongatus with a postcrystallization treatment involving extraction of the detergent C12E8. This resulted in a transition from Type II to Type I-like membrane protein crystals and improved diffraction to 2.44 Å resolution. The obtained PSII packing in precise rows, interconnected by specific pairs of galactolipids and a loop in the PsbO subunit specific to cyanobacteria, is superimposable with previous electron microscopy images of the thylakoid membrane. The study provides a detailed model of such a superstructure and its organization of light-harvesting pigments with possible implications for the understanding of their efficient use of solar energy.
PubMed: 25438669
DOI: 10.1016/j.str.2014.09.007
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.437 Å)
Structure validation

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