Interdomain Disulfide Bridge in the Rice Granule Bound Starch Synthase I Catalytic Domain as Elucidated by X-Ray Structure Analysis
Interdomain Disulfide Bridge in the Rice Granule Bound Starch Synthase I Catalytic Domain as Elucidated by X-Ray Structure Analysis
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DOI：
10.1271/bbb.120305
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发表时间：
2012-08-01
影响因子：
1.6
通讯作者：
Fujimoto, Zui
中科院分区：
文献类型：
--
作者：
Momma, Mitsuru;Fujimoto, Zui
水稻 (Oryza sativa japonica) 颗粒结合淀粉合酶 I (OsGBSSI-CD) 的催化结构域被过表达，并确定了无配体和 ADP 结合形式的三维结构。这些结构与报道的细菌和古菌糖原合酶类似，属于糖基转移酶家族 5。它们具有通过典型双铰链肽连接的罗斯曼折叠 N 和 C 结构域，以及似乎在禾本科植物家族中保守的结构域间二硫键。三个共价键的存在可以解释为什么两种 OsGBSSI-CD 结构仅采用封闭域排列。
The catalytic domain of rice (Oryza sativa japonica) granule bound starch synthase I (OsGBSSI-CD) was overexpressed and the three-dimensional structures of the ligand-free and ADP-bound forms were determined. The structures were similar to those reported for bacterial and archaeal glycogen synthases, which belong to glycosyltransferase family 5. They had Rossmann fold N- and C-domains connected by canonical two-hinge peptides, and an interdomain disulfide bond that appears to be conserved in the Poaceae plant family. The presence of three covalent linkages might explain why both OsGBSSI-CD structures adopted only the closed domain arrangement.