Ficner R, Huber R
Max-Planck-Institut für Biochemie, Martinsried, Germany.
Eur J Biochem. 1993 Nov 15;218(1):103-6. doi: 10.1111/j.1432-1033.1993.tb18356.x.
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 (alpha beta)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 (alpha beta)6 aggregate.
已在0.23纳米分辨率下确定了来自红海紫菜的捕光色素蛋白b-藻红蛋白的三维结构。b-藻红蛋白的结构与来自污红藻的B-藻红蛋白的结构非常相似。除了三个不同的残基外，b-藻红蛋白与B-藻红蛋白的α和β亚基之间分别只有很小的差异。在晶体中，b-藻红蛋白形成一个(αβ)6六聚体（分子量：236 kDa），而B-藻红蛋白还含有一个30 kDa的γ亚基。b-藻红蛋白和B-藻红蛋白电子密度图的比较清楚地表明，γ亚基位于(αβ)6聚集体内部。
