1H, 13C and 15N resonance assignments of the chaperone HybE of hydrogenase-2 from Escherichia coli.
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.
Shao
Xuan
X
Beijing Nuclear Magnetic Resonance Center, Peking University, 100871, Beijing, China.
Lu
Jie
J
Xia
Bin
B
Jin
Changwen
C
D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006864:Hydrogenase / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D018832:Molecular Chaperones / Q000737:chemistry*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011522:Protons
D002247:Carbon Isotopes; D029968:Escherichia coli Proteins; C544446:HybE protein, E coli; D018832:Molecular Chaperones; D009587:Nitrogen Isotopes; D021122:Protein Subunits; D011522:Protons; D006864:Hydrogenase; C481721:hydrogenase 2, E coli