1H, 13C and 15N resonance assignments of the chaperone HybE of hydrogenase-2 from Escherichia coli

被引：1

作者：

Shao, Xuan ^{[1
,3
]}

Lu, Jie ^{[1
,2
]}

Xia, Bin ^{[1
,2
,3
]}

Jin, Changwen ^{[1
,2
,3
]}

机构：

[1] Peking Univ, Beijing Nucl Magnet Resonance Ctr, Beijing 100871, Peoples R China

[2] Peking Univ, Coll Life Sci, Beijing 100871, Peoples R China

[3] Peking Univ, Coll Chem & Mol Engn, Beijing 100871, Peoples R China

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2009年 / 3卷 / 01期

关键词：

Escherichia coli; HybE; Assignments; NMR; Chemical shift; PROTEINS; PATHWAY; EXPORT; IDENTIFICATION; SYSTEM;

D O I：

10.1007/s12104-009-9157-5

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

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 H-1, C-13 and (15) N atoms in E. coli HybE.

引用

页码：129 / 131

页数：3

共 13 条

[1] Protein targeting by the bacterial twin-arginine translocation (Tat) pathway [J].