Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.10.3.9 extracted from

  • Zobnina, V.; Lambreva, M.D.; Rea, G.; Campi, G.; Antonacci, A.; Scognamiglio, V.; Giardi, M.T.; Polticelli, F.
    The plastoquinol-plastoquinone exchange mechanism in photosystem II insight from molecular dynamics simulations (2017), Photosynth. Res., 131, 15-30 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular dynamics simulations of the complete PSII complex embedded in a lipid bilayer. PSII in the presence of plastoquinol shows a distinct dynamic behaviour which causes disruption of the interactions seen in the PSII-plastoquinone complex and leads to release of plastoquinol from the binding pocket. Displacement of plastoquinol closes the second water channel. Residue D1-Ser264 has a pivotal role in modulating the dynamics of the plastoquinone binding pocket and plastoquinol-plastoquinone exchange via its interaction with residue D1-His252 Thermosynechococcus vestitus

Protein Variants

Protein Variants Comment Organism
S264K mutation in protein D1. Mutant displays a severe and persistent hampering of the QA-QB electron transfer resulting in a delay of the plastoquinone pool reduction rate Thermosynechococcus vestitus

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Thermosynechococcus vestitus P0A444
-
-

Synonyms

Synonyms Comment Organism
photosystem II protein D1 1
-
Thermosynechococcus vestitus
PsbA1
-
Thermosynechococcus vestitus