Assignment of (1)H, (13)C, and (15)N resonances of YgiT, a putative DNA interacting protein from E. coli, containing one HTH and two CxxC motifs.
The 131 residues protein encoded by the open reading frame ygiT of E. coli contains two characteristic domains: a zinc finger protein-like structure with two CxxC motives at its N-terminus and a helix-turn-helix (HTH) motif at its C-terminus. We report the backbone and side chain (1)H, (13)C, and (15)N resonances assignment of YgiT.
Papadopoulos
Evangelos
E
Department of Biochemistry and Biophysics, Stockholm University, Sweden.
Billeter
Martin
M
Gräslund
Astrid
A
Vlamis-Gardikas
Alexios
A
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011522:Protons
D002247:Carbon Isotopes; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C555039:MqsA protein, E coli; D009587:Nitrogen Isotopes; D011522:Protons