Crystallization (Comment) | Organism |
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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 | Comment | Organism |
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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 | Comment | Organism | GeneOntology No. | Textmining |
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Organism | UniProt | Comment | Textmining |
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Thermosynechococcus vestitus | P0A444 | - |
- |
Synonyms | Comment | Organism |
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photosystem II protein D1 1 | - |
Thermosynechococcus vestitus |
PsbA1 | - |
Thermosynechococcus vestitus |