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External and internal electrostatic potentials of cholinesterase models

C E Felder1, S A Botti, S Lifson

  • 1Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.

Journal of Molecular Graphics & Modelling
|June 26, 1998
PubMed
Summary

Cholinesterases possess a conserved negative electrostatic potential within their active-site gorge. This conserved charge distribution in acetylcholinesterase and butyrylcholinesterase likely guides substrates to the active site.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Chemistry

Background:

  • Cholinesterases are crucial enzymes involved in neurotransmission and detoxification.
  • Understanding the structure-function relationship of cholinesterases is vital for drug development.
  • Electrostatic properties play a significant role in enzyme-substrate interactions.

Purpose of the Study:

  • To calculate and analyze the electrostatic potentials of various cholinesterase structures.
  • To identify conserved electrostatic features across different species.
  • To elucidate the role of electrostatic potentials in cholinesterase function and substrate binding.

Main Methods:

  • Utilized the Delphi algorithm based on the Poisson-Boltzmann equation for electrostatic potential calculations.

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  • Employed experimentally determined structures of Torpedo californica and mouse acetylcholinesterase.
  • Generated homology models for human, Bungarus fasciatus, and Drosophila melanogaster acetylcholinesterases, and human butyrylcholinesterase.

    • Main Results:

    • All analyzed cholinesterase structures exhibited a negative surface potential near the active-site gorge entrance, intensifying towards the gorge rim.
    • A progressively more negative potential was observed along the gorge's central axis, peaking at the active site.
    • Ten conserved acidic residues were identified as primary contributors to these conserved electrostatic potentials.

    Conclusions:

    • The calculated electrostatic potentials are a conserved feature across the cholinesterase family, even with low sequence identity.
    • The negative potential likely functions to attract positively charged substrates into the active-site gorge.
    • These conserved electrostatic properties may be critical for cholinesterase catalytic activity and other functions.