1H, 13C and 15N resonance assignments of the rhodanese domain of YgaP from Escherichia coli.
Rhodanese domain is a ubiquitous structural module commonly found in bacterial, archaeal and eukaryotic cells. Growing evidence indicates that rhodanese domains act as the carrier of reactive sulfur atoms by forming persulfide intermediates in distinct metabolic pathways. YgaP, a membrane protein consisting of a rhodanese domain and a C-terminal transmembrane segment, is the only membrane-associated rhodanese in Escherichia coli. Herein, we report the resonance assignments of (1)H, (13)C and (15)N atoms of rhodanese domain of YgaP. Totally, chemical shifts of more than 95% of the atoms were assigned.
Beijing Nuclear Magnetic Resonance Center, Peking University, China.
Hongwei
H
Li
Yunchen
Y
Bi
Bin
B
Xia
Changwen
C
Jin
D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006859:Hydrogen; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D013884:Thiosulfate Sulfurtransferase / Q000737:chemistry*
D002247:Carbon Isotopes; D029968:Escherichia coli Proteins; D009587:Nitrogen Isotopes; C530142:YgaP protein, E coli; D006859:Hydrogen; D013884:Thiosulfate Sulfurtransferase