大肠杆菌氢化酶-2伴侣蛋白HybE的1H、13C和15N共振归属
1H, 13C and 15N resonance assignments of the chaperone HybE of hydrogenase-2 from Escherichia coli.
作者信息
Shao Xuan, Lu Jie, Xia Bin, Jin Changwen
机构信息
Beijing Nuclear Magnetic Resonance Center, Peking University, 100871, Beijing, China.
出版信息
Biomol NMR Assign. 2009 Jun;3(1):129-31. doi: 10.1007/s12104-009-9157-5. Epub 2009 Apr 3.
Escherichia coli HybE is a chaperone of hydrogenase-2 and plays a critical role in coordinating the assembly and export of the HybO and HybC subunits of hydrogenase-2. Previous studies indicated that the quality-control during the assembly and export of the HybO-HybC by the Tat pathway was putatively performed by HybE. However, the molecular basis of the biological function of HybE remains unknown. The structural information is essential in order to obtain functional insights of HybE. Here we report the backbone and sidechain resonance assignments of (1)H, (13)C and (15) N atoms in E. coli HybE.
大肠杆菌HybE是氢化酶-2的伴侣蛋白，在协调氢化酶-2的HybO和HybC亚基的组装和输出中起关键作用。先前的研究表明，Tat途径在HybO-HybC组装和输出过程中的质量控制可能由HybE执行。然而，HybE生物学功能的分子基础仍然未知。为了深入了解HybE的功能，结构信息至关重要。在此，我们报告了大肠杆菌HybE中(1)H、(13)C和(15)N原子的主链和侧链共振归属。
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