Subunit positioning and transmembrane helix organisation in the core dimer of photosystem II

FEBS Letters

Hankamer, Ben²  Nield, Jon²  Morris, Ed²  Barber, James²  Carne, Alex¹ 

[1] Institute of Cancer Research, Chester Beatty Laboratories, London SW3 6JB, UK;Wolfson Laboratories, Department of Biological Sciences, Imperial College of Science, Technology and Medicine, London SW7 2AY, UK

关键词: Photosynthesis;    Photosystem II;    Structure;    Electron microscopy;    X-ray diffraction;    Low molecular weight subunit;   

DOI  :  10.1016/S0014-5793(01)02766-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown