Subunit positioning and transmembrane helix organisation in the core dimer of photosystem II.
Recently 3D structural models of the photosystem II (PSII) core dimer complexes of higher plants (spinach) and cyanobacteria (Synechococcus elongatus) have been derived by electron [Rhee et al. (1998) Nature 396, 283-286; Hankamer et al. (2001) J. Struct. Biol., in press] and X-ray [Zouni et al. (2001) Nature 409, 739-743] crystallography respectively. The intermediate resolutions of these structures do not allow direct identification of side chains and therefore many of the individual subunits within the structure are unassigned. Here we review the structure of the higher plant PSII core dimer and provide evidence for the tentative assignment of the low molecular weight subunits. In so doing we highlight the similarities and differences between the higher plant and cyanobacterial structures.
Hankamer
B
B
Department of Biological Sciences, Imperial College of Science, Technology and Medicine, London, UK.
Morris
E
E
Nield
J
J
Carne
A
A
Barber
J
J
D002462:Cell Membrane / Q000737:chemistry*; D002734:Chlorophyll / Q000737:chemistry; D018360:Crystallography, X-Ray; D019281:Dimerization; D045342:Light-Harvesting Protein Complexes; D008954:Models, Biological; D008958:Models, Molecular; D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism*; D045332:Photosystem II Protein Complex; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D002734:Chlorophyll