Modeling the antiferromagnetic MnIIMnII system within the protein phosphatase-5 catalytic site

J Mol Model. 2015 Jan;21(1):14. doi: 10.1007/s00894-014-2556-2. Epub 2015 Jan 24.

Abstract

Protein phosphatase-5 (PP5), a novel target for inhibition in a search for new antitumor drugs, contains a homobimetallic Mn(II)Mn(II) system in its catalytic site. The ground electronic state is an antiferromagnetically-coupled singlet. We report optimizations of a known inhibitor within a 42-residue model of the PP5 catalytic site under several two-level hybrid ONIOM computational models. Using the high-resolution crystal structure of a PP5/inhibitor complex as reference, we compare geometric parameters as the qualities of the "high-level" and "low-level" wavefunctions are successively improved by using the correct antiferromagnetic (AF) singlet state. We find that the UB3LYP AF wavefunction for the high-level region is necessary for experimental fidelity. A closed-shell semi-empirical method (RPM6) can be used for the low-quality part of the hybrid scheme to afford geometries which are qualitatively on par with that obtained using the more time-consuming open-shell UB3LYP AF wavefunction. As the AF state can be elusive for such a large system, the ferromagnetic (F) state can also be used in the low-quality calculations without impacting the geometry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalytic Domain*
  • Enzyme Inhibitors / chemistry*
  • Manganese / chemistry*
  • Models, Molecular*
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / metabolism
  • Phosphoprotein Phosphatases / chemistry*
  • Phosphoprotein Phosphatases / metabolism

Substances

  • Enzyme Inhibitors
  • Nuclear Proteins
  • Manganese
  • Phosphoprotein Phosphatases
  • protein phosphatase 5