Crystal structures of the ribonuclease MC1 from bitter gourd seeds, complexed with 2'-UMP or 3'-UMP, reveal structural basis for uridine specificity.

@article{Suzuki2000CrystalSO,
  title={Crystal structures of the ribonuclease MC1 from bitter gourd seeds, complexed with 2'-UMP or 3'-UMP, reveal structural basis for uridine specificity.},
  author={Akira John Suzuki and Min Liang Yao and I Tanaka and Tomoyuki Numata and Shingo Kikukawa and Nobuyuki Yamasaki and Makoto Kimura},
  journal={Biochemical and biophysical research communications},
  year={2000},
  volume={275 2},
  pages={
          572-6
        }
}
Ribonuclease MC1 (RNase MC1) isolated from seeds of bitter gourd (Momordica charantia) consists of 190 amino acids and is characterized by a preferential cleavage at the 5'-side of uridine. This uridine specificity distinguishes RNase MC1 from other enzymes belonging to the RNase T2 family. The three-dimensional structures of RNase MC1, in a complex with either 2'-UMP or 3'-UMP, were determined at 1.48 and 1.77 A resolutions, respectively. The side chains of Gln9 and Asn71 interact with O4 and… CONTINUE READING

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