1. Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach.
- Author
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Boetsch C, Aguayo-Villegas DR, Gonzalez-Nilo FD, Lisa ÁT, and Beassoni PR
- Subjects
- Binding Sites, Catalytic Domain, Hydrogen chemistry, Kinetics, Molecular Conformation, Molecular Dynamics Simulation, Mutagenesis, Site-Directed, Mutation, Polyphosphates chemistry, Protein Binding, Static Electricity, Thermodynamics, Acid Anhydride Hydrolases chemistry, Bacterial Proteins chemistry, Escherichia coli metabolism
- Abstract
The exopolyphosphatase of Escherichia coli processively and completely hydrolyses long polyphosphate chains to ortho-phosphate. Genetic surveys, based on the analysis of single ppx(-) or ppk(-) mutants and on the double mutant, demonstrate a relationship between these genes and the survival capacity. The exopolyphosphatase belongs to the ASKHA protein superfamily, hence, its active site is well known; however, the knowledge of the way in which this enzyme binds polyP remains incomplete. Here we present different computational approaches, site-direct mutagenesis and kinetic data to understand the relationship between structure and function of exopolyphosphatase. We propose H(378) as a fundamental gatekeeper for the recognition of long chain polyphosphate., (Copyright © 2016. Published by Elsevier Inc.)
- Published
- 2016
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