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

Resultado de la investigación: Contribución a una revistaArtículo

1 Cita (Scopus)

Resumen

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.

Idioma originalInglés
Páginas (desde-hasta)64-72
Número de páginas9
PublicaciónArchives of Biochemistry and Biophysics
Volumen606
DOI
EstadoPublicada - 15 sep 2016

Áreas temáticas de ASJC Scopus

  • Biofísica
  • Bioquímica
  • Biología molecular

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