Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F
Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F
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DOI：
10.1038/nsmb.2918
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发表时间：
2014-12-01
影响因子：
16.8
通讯作者：
Locher, Kaspar P.
中科院分区：
文献类型：
--
作者：
Korkhov, Vladimir M.;Mireku, Samantha A.;Locher, Kaspar P.
BtuCD-F催化维生素B12转运到大肠杆菌中的反应机制目前尚不清楚。在这里，我们提出了最后一个缺失状态的结构，在AMP-PNP结合BtuCD的形式，被二硫键交联捕获。我们的结构和生化数据允许制定一致的机制，从而合理化的作用，底物，ATP和底物结合蛋白。
The reaction mechanism of BtuCD-F-catalyzed vitamin B12 transport into Escherichia coli is currently unclear. Here we present the structure of the last missing state in the form of AMP-PNP-bound BtuCD, trapped by a disulfide cross-link. Our structural and biochemical data allow a consistent mechanism to be formulated, thus rationalizing the roles of substrate, ATP and substrate-binding protein.