来自嗜热蓝藻的C-藻蓝蛋白晶体结构为藻胆体组装提供了新视角。
Crystal structure of C-phycocyanin from Cyanidium caldarium provides a new perspective on phycobilisome assembly.
作者信息
Stec B, Troxler R F, Teeter M M
机构信息
Department of Chemistry, Merkert Chemistry Building, Boston College, Chestnut Hill, Massachusetts 02167, USA.
出版信息
Biophys J. 1999 Jun;76(6):2912-21. doi: 10.1016/S0006-3495(99)77446-1.
Abstract
The crystal structure of the light-harvesting protein phycocyanin from the cyanobacterium Cyanidium caldarium with novel crystal packing has been solved at 1.65-A resolution. The structure has been refined to an R value of 18.3% with excellent backbone and side-chain stereochemical parameters. In crystals of phycocyanin used in this study, the hexamers are offset rather than aligned as in other phycocyanins that have been crystallized to date. Analysis of this crystal's unique packing leads to a proposal for phycobilisome assembly in vivo and for a more prominent role for chromophore beta-155. This new role assigned to chromophore beta-155 in phycocyanin sheds light on the numerical relationships among and function of external chromophores found in phycoerythrins and phycoerythrocyanins.
摘要
已通过1.65埃的分辨率解析了来自嗜热蓝藻（Cyanidium caldarium）的具有新型晶体堆积的捕光蛋白藻蓝蛋白的晶体结构。该结构已精修至R值为18.3%，具有出色的主链和侧链立体化学参数。在本研究中使用的藻蓝蛋白晶体中，六聚体是错位的，而不是像迄今为止已结晶的其他藻蓝蛋白那样排列整齐。对这种晶体独特堆积的分析为藻胆体在体内的组装以及生色团β-155发挥更突出的作用提出了一个建议。赋予藻蓝蛋白中生色团β-155的这一新作用揭示了藻红蛋白和藻红青蛋白中外部生色团之间的数量关系及其功能。
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