Three-dimensional structures of C-phycocyanin and B-phycoerythrin at 5-A resolution.
作者： R.G. Fisher , N.E. Woods , H.E. Fuchs , R.M. Sweet
DOI: 10.1016/S0021-9258(19)70752-2
关键词:
摘要: Single crystal x-ray diffraction studies are proceeding on two phycobiliproteins: C-Phycocyanin from Anabaena variabilis and B-Phycoerythrin Porphyridium cruentum. consists of six alpha beta subunits. A three-dimensional study this light-harvesting protein (P6(3); a = b 154.1 A, c 40.1 A) at 5-A resolution shows that the molecule is 110 in diameter, 40 thick, with 20-A diameter central channel. It can be divided into three separate domains related by crystallographic 3 contains long, columnar regions density, presumed to represent helix. composed 6 alpha, beta, gamma subunit. 5.25-A (R3, 189 60 indicates 107 55 has 32-D3 symmetry, regions. The chain lies undergoes symmetric disordering. region low unstructured density center presumably occupied chains. These structures compared regard differences quaternary structure.
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