Requirements for different combinations of the extrinsic proteins in specific cyanobacterial photosystem II mutants.
The crystallographic data available for Photosystem II (PS II) in cyanobacteria has now provided complete structures for loop E from CP43 and CP47 as well as the extrinsic subunits PsbO, PsbU and PsbV. Protein interactions between these subunits are essential for stable water splitting and there is evidence that the binding of PsbU facilitates optimal energy transfer from the phycobilisome. Interactions between PsbO and CP47 may also play a role in dimer stabilization while loop E of CP43 contributes directly to the water-splitting reaction. Recent evidence also suggests that homologs of PsbP and PsbQ play key roles in cyanobacterial PS II, and under nutrient-deficient conditions PsbQ appears essential for photoautotrophic growth.
Eaton-Rye
Julian J
JJ
Department of Biochemistry, University of Otago, P.O. Box 56, Dunedin, New Zealand. julian.eaton-rye@stonebow.otago.ac.nz
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D009154:Mutation / Q000235:genetics*; D045332:Photosystem II Protein Complex / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D046939:Synechocystis / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes; D045332:Photosystem II Protein Complex; C107126:PsbU protein, Synechocystis; C070970:photosystem II, chlorophyll-binding protein, CP-47