Literature summary for 1.10.3.9 extracted from

Endo, K.; Kobayashi, K.; Wang, H.T.; Chu, H.A.; Shen, J.R.; Wada, H.
Site-directed mutagenesis of two amino acid residues in cytochrome b559 alpha subunit that interact with a phosphatidylglycerol molecule (PG772) induces quinone-dependent inhibition of photosystem II activity (2019), Photosynth. Res., 139, 267-279 .

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Protein Variants

Protein Variants	Comment	Organism
S11A	mutation in the cytochrome (Cyt) b559 alpha subunit. Photosynthetic activity of intact cells is slightly lower in mutant than that of cells in the control strain. One phosphatidylglycerol molecule per reaction center (presumably PG772), is lost in the photosystem II (PSII) dimer. The site-directed mutagenesis of Thr5 and Ser11 induces quinone-dependent inhibition of PSII activity under high-intensity light conditions and destabilizes the binding of extrinsic proteins to PSII	Synechocystis sp. PCC 6803
T5A	mutation in the cytochrome (Cyt) b559 alpha subunit. Photosynthetic activity of intact cells is slightly lower in mutant than that of cells in the control strain. One phosphatidylglycerol molecule per reaction center (presumably PG772), is lost in the photosystem II (PSII) dimer. The site-directed mutagenesis of Thr5 and Ser11 induces quinone-dependent inhibition of PSII activity under high-intensity light conditions and destabilizes the binding of extrinsic proteins to PSII	Synechocystis sp. PCC 6803

Organism

Organism	UniProt	Comment	Textmining
Synechocystis sp. PCC 6803	P09190	cytochrome b559 subunit alpha, photosystem II reaction center subunit V	-

Synonyms

Synonyms	Comment	Organism
PSII	-	Synechocystis sp. PCC 6803

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Release 2023.1 (January 2023)