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: Article

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

Huella dactilar

Polyphosphates
Computer Simulation
Mutagenesis
Polyps
Hydrolysis
Catalytic Domain
Genes
Phosphates
Kinetics
Enzymes
Proteins
Escherichia coli Ppx protein
exopolyphosphatase
Surveys and Questionnaires

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

Citar esto

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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.",
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T1 - Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach

AU - Boetsch, Cristhian

AU - Aguayo-Villegas, Daniel R.

AU - Gonzalez-Nilo, Fernando D.

AU - Lisa, Teresita

AU - Beassoni, Paola R.

PY - 2016/9/15

Y1 - 2016/9/15

N2 - 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.

AB - 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.

KW - Binding

KW - Exopolyphosphatase

KW - Molecular dynamics

KW - Polyphosphate

KW - Processivity

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DO - 10.1016/j.abb.2016.07.005

M3 - Article

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SP - 64

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JO - Archives of Biochemistry and Biophysics

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