1H, 13C and 15N resonance assignments of rhodanese GlpE from Escherichia coli.
Rhodanese catalyzes the sulfur-transfer reaction in which a sulfur atom is transferred from thiosulfate to cyanide by a double-displacement mechanism. During the reaction, a persulfide-intermediate form of rhodanese is generated by the reaction of a conserved active cysteine residue with thiosulfate. Escherichia coli GlpE is a prototype for the single-domain rhodanese superfamily. Though there are some studies on rhodaneses, the molecular mechanism of the catalytic activity of rhodaneses is still unclear. Herein, we report the resonance assignments of (1)H, (13)C and (15)N atoms of E. coli GlpE, which provides the basis for further structural, dynamic and functional studies of rhodaneses using NMR technique.
Beijing Nuclear Magnetic Resonance Center, Peking University, China.
Hongwei
H
Li
Bin
B
Xia
Changwen
C
Jin
D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006859:Hydrogen; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D013884:Thiosulfate Sulfurtransferase / Q000737:chemistry*
D002247:Carbon Isotopes; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C102897:GlpE protein, E coli; D009587:Nitrogen Isotopes; D006859:Hydrogen; D013884:Thiosulfate Sulfurtransferase