Literature summary for 1.10.3.9 extracted from

Endo, K.; Mizusawa, N.; Shen, J.R.; Yamada, M.; Tomo, T.; Komatsu, H.; Kobayashi, M.; Kobayashi, K.; Wada, H.
Site-directed mutagenesis of amino acid residues of D1 protein interacting with phosphatidylglycerol affects the function of plastoquinone QB in photosystem II (2015), Photosynth. Res., 126, 385-397 .

Search for more literature for 1.10.3.9

Cloned(Commentary)

Cloned (Comment)	Organism
-	Synechocystis sp. PCC 6803

Protein Variants

Protein Variants	Comment	Organism
N234D	mutation of residue that interacts with two of the phosphatidylglycerol molecules of the complex. Mutant exhibits normal growth, but shows decreased photosynthetic activities and slower electron transport from QA to QB than the control strain	Synechocystis sp. PCC 6803
S232A	mutation of residue that interacts with two of the phosphatidylglycerol molecules of the complex. Mutant exhibits normal growth, but shows decreased photosynthetic activities and slower electron transport from QA to QB than the control strain	Synechocystis sp. PCC 6803
S232A/N234D	mutation of residues that interact with two of the phosphatidylglycerol molecules of the complex. Mutant exhibits normal growth, but shows decreased photosynthetic activities and slower electron transport from QA to QB than the control strain. The levels of extrinsic proteins, PsbV and PsbU, are decreased in PSII monomers, while that of Psb28 is increased. The content of phosphatidylglycerol in PSII is slightly decreased, whereas that of monogalactosyldiacylglycerol is increased	Synechocystis sp. PCC 6803

Organism

Organism	UniProt	Comment	Textmining
Synechocystis sp. PCC 6803	P16033	-	-

Synonyms

Synonyms	Comment	Organism
photosystem II protein D1 2	-	Synechocystis sp. PCC 6803
PsbA2	-	Synechocystis sp. PCC 6803

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)