Structural analysis of a multifunctional, tandemly repeated inositol polyphosphatase.

@article{Gruninger2009StructuralAO,
  title={Structural analysis of a multifunctional, tandemly repeated inositol polyphosphatase.},
  author={Robert J. Gruninger and L. Brent Selinger and Steven C. Mosimann},
  journal={Journal of molecular biology},
  year={2009},
  volume={392 1},
  pages={75-86}
}
Mitsuokella multacida expresses a unique inositol polyphosphatase (PhyAmm) that is composed of tandem repeats (TRs). Each repeat possesses a protein tyrosine phosphatase (PTP) active-site signature sequence and fold. Using a combination of structural, mutational, and kinetic studies, we show that the N-terminal (D1) and C-terminal (D2) active sites of the TR have diverged and possess significantly different specificities for inositol polyphosphate. Structural analysis and molecular docking… CONTINUE READING