Structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 A resolution.
Structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 A resolution.
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来自集胞藻的 D-核酮糖 5-磷酸 3-差向异构酶的结构，分辨率为 1.6 A。
DOI：
10.1107/s0907444904015896
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发表时间：
2004
期刊：
影响因子：
--
通讯作者：
Rayment,Ivan
中科院分区：
文献类型：
--
作者：
Wise,EricL;Akana,Julie;Gerlt,JohnA;Rayment,Ivan
采用1.6 Å分辨率的x射线晶体学方法对蓝细菌聚囊藻（Synechocystis）的d-核酮糖5-磷酸3- epimase （RPE）的晶体结构进行了研究。该酶催化5-磷酸d-核酮糖和5-磷酸d-木酮糖的外映异构，在晶体不对称单元中组装成（β/α）8-桶的六聚体。活性位点与先前报道的两种rpe高度相似，并进一步证明了几种活性位点残基的基本催化作用。
The crystal structure of d-ribulose 5-phosphate 3-epimerase (RPE) from the cyanobacterium Synechocystis was determined by X-ray crystallography to 1.6 Å resolution. The enzyme, which catalyzes the epimerization of d-ribulose 5-phosphate and d-xylulose 5-phosphate, assembles as a hexamer of (β/α)8-barrels in the crystallographic asymmetric unit. The active site is highly similar to those of two previously reported RPEs and provides further evidence for essential catalytic roles for several active-site residues.