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

被引:69
作者
Hankamer, B
Morris, E
Nield, J
Carne, A
Barber, J [1 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, Wolfson Labs, Dept Sci Biol, London SW7 2AY, England
[2] Inst Canc Res, Chester Beatty Labs, London SW3 6JB, England
来源
FEBS LETTERS | 2001年 / 504卷 / 03期
关键词
photosynthesis; photosystem II; structure; electron microscopy; X-ray diffraction; low molecular weight subunit;
D O I
10.1016/S0014-5793(01)02766-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:142 / 151
页数:10
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