TETRAMERIC NATIVE STRUCTURE OF THE PERIDININ-CHLOROPHYLL A-BINDING PROTEIN FROM SYMBIODINIUM SP

被引：7

作者：

GERBERDING, H ^{[1
]}

NORRIS, B ^{[1
]}

MILLER, DJ ^{[1
]}

MAYER, F ^{[1
]}

机构：

[1] JAMES COOK UNIV N QUEENSLAND,DEPT CHEM & BIOCHEM,TOWNSVILLE,QLD 4811,AUSTRALIA

来源：

JOURNAL OF PLANT PHYSIOLOGY | 1991年 / 137卷 / 03期

关键词：

D O I：

10.1016/S0176-1617(11)80132-X

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

Electron microscopy of a single isoform of the peridinin-chlorophyll a-binding protein from Symbiodinium sp. indicates that the native structure is a tetrahedron-like assembly of four subunits. The subunits are elongated and have a somewhat bent appearance. Based on the EM observations, a working model is proposed that has two orthogonally-arranged dimers in contact via their concave surfaces.

引用

页码：285 / 290

页数：6

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