REFINED CRYSTAL-STRUCTURE OF PHYCOERYTHRIN FROM PORPHYRIDIUM-CRUENTUM AT 0.23-NM RESOLUTION AND LOCALIZATION OF THE GAMMA-SUBUNIT

被引:77
作者
FICNER, R
HUBER, R
机构
[1] Max-Planck-Institut Für Biochemie, Martinsried
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1993年 / 218卷 / 01期
关键词
D O I
10.1111/j.1432-1033.1993.tb18356.x
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
The three-dimensional structure of the light-harvesting pigment-protein b-phycoerythrin from the red alga Porphyridium cruentum has been determined at 0.23-nm resolution. The b-phycoerythrin structure is very similar to the structure of B-phycoerythrin from Porphyridium sordidum. Besides three non-identical residues there are only small differences between b-phycoerythrin and B-phycoerythrin alpha and beta subunits, respectively. In the crystals b-phycoerythrin forms an (alphabeta)6 hexamer (molecular mass: 236 kDa), whereas B-phycoerythrin additionally contains a 30-kDa gamma subunit. The comparison of the b-phycoerythrin and B-phycoerythrin electron-density maps clearly reveals, that the gamma subunit is located inside the (alphabeta)6 aggregate.
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页码:103 / 106
页数:4
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