Structure of CcmG/DsbE at 1.14 Å resolution:: High-fidelity reducing activity in an indiscriminately oxidizing environment
Structure of CcmG/DsbE at 1.14 Å resolution:: High-fidelity reducing activity in an indiscriminately oxidizing environment
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DOI：
10.1016/s0969-2126(02)00794-3
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发表时间：
2002-07-01
期刊：
影响因子：
5.7
通讯作者：
Martin, JL
中科院分区：
文献类型：
--
作者：
Edeling, MA;Guddat, LW;Martin, JL
CCMG不同于其他类似硫氧还蛋白(TRX)的蛋白质，因为它在氧化环境中具有特定的还原活性，并且相互作用的保真度很高。这两个不同寻常的特性是它在C型细胞色素成熟中所必需的。CCMG的晶体结构显示了一个具有异常酸性活性中心的改性TrX折叠和由折叠中的两个插入物形成的凹槽。删除其中一个形成槽的插入物会破坏C型细胞色素的形成。CCMG的两个独特的结构特征-酸性活性部位和相邻的凹槽-似乎是将不分青红皂白结合的支架TRX折叠转化为高度特异的氧化还原蛋白所必需的。
CcmG is unlike other periplasmic thioredoxin (TRX)like proteins in that it has a specific reducing activity in an oxidizing environment and a high fidelity of interaction. These two unusual properties are required for its role in c-type cytochrome maturation. The crystal structure of CcmG reveals a modified TRX fold with an unusually acidic active site and a groove formed from two inserts in the fold. Deletion of one of the groove-forming inserts disrupts c-type cytochrome formation. Two unique structural features of CcmG-an acidic active site and an adjacent groove-appear to be necessary to convert an indiscriminately binding scaffold, the TRX fold, into a highly specific redox protein.