Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach

Cristhian Boetsch, Daniel R. Aguayo-Villegas, Fernando D. Gonzalez-Nilo, Teresita Lisa, Paola R. Beassoni

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

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 H378 as a fundamental gatekeeper for the recognition of long chain polyphosphate.

Original languageEnglish
Pages (from-to)64-72
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume606
DOIs
Publication statusPublished - 15 Sep 2016

Keywords

  • Binding
  • Exopolyphosphatase
  • Molecular dynamics
  • Polyphosphate
  • Processivity

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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