The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad.

@article{Rydel2003TheCS,
  title={The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid acyl hydrolase with a Ser-Asp catalytic dyad.},
  author={Timothy J. Rydel and Jennifer M. Williams and Elysia K Krieger and Farhad Moshiri and William C. Stallings and Sherri M. Brown and Jay C Pershing and John P Purcell and Murtaza F Alibhai},
  journal={Biochemistry},
  year={2003},
  volume={42 22},
  pages={6696-708}
}
Patatin is a nonspecific lipid acyl hydrolase that accounts for approximately 40% of the total soluble protein in mature potato tubers, and it has potent insecticidal activity against the corn rootworm. We determined the X-ray crystal structure of a His-tagged variant of an isozyme of patatin, Pat17, to 2.2 A resolution, employing SeMet multiwavelength anomalous dispersion (MAD) phasing methods. The patatin crystal structure has three molecules in the asymmetric unit, an R-factor of 22.0%, and… CONTINUE READING
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