Prediction of structure of antenna proteins of photosystem II.
Membrane spanning regions of 43 kDa and 47 kDa antenna proteins of photosystem II of thylakoid membranes are theoretically predicted. Prediction of topology of chlorophyll-a and beta-carotene molecules in the proteins and interaction of the proteins with 33 kDa extrinsic protein on the lumenal side of thylakoid membrane is based on the findings reported earlier. Each antenna protein is predicted to have six transmembrane alpha-helices with twelve chlorophyll-a and five beta-carotene molecules binding to it. Both N- and C- terminal ends are proposed to be on the stromal side of thylakoid membrane. The proposed structural model conforms to the reported experimental results from the literature.
Raval
M K
MK
Post Graduate Department of Chemistry, Rajendra College, Orissa, India.
Rath
L S
LS
D001665:Binding Sites; D002734:Chlorophyll / Q000032:analysis; D000077194:Chlorophyll A; D007425:Intracellular Membranes / Q000737:chemistry; D045342:Light-Harvesting Protein Complexes; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008970:Molecular Weight; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D045332:Photosystem II Protein Complex; D017433:Protein Structure, Secondary; D019207:beta Carotene / Q000032:analysis
D045342:Light-Harvesting Protein Complexes; D008565:Membrane Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D019207:beta Carotene; D002734:Chlorophyll; D000077194:Chlorophyll A