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: Research - revisión exhaustivaArticle

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.

IdiomaEnglish
Páginas64-72
Número de páginas9
PublicaciónArchives of Biochemistry and Biophysics
Volumen606
DOI
EstadoPublished - 15 sep 2016

Huella dactilar

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

Keywords

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Medicine(all)
    • Molecular Biology

    Citar esto

    @article{6902ceed56a4453b8ff82c07b6003e5f,
    title = "Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach",
    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.",
    keywords = "Binding, Exopolyphosphatase, Molecular dynamics, Polyphosphate, Processivity",
    author = "Cristhian Boetsch and Aguayo-Villegas, {Daniel R.} and Gonzalez-Nilo, {Fernando D.} and Teresita Lisa and Beassoni, {Paola R.}",
    year = "2016",
    month = "9",
    doi = "10.1016/j.abb.2016.07.005",
    volume = "606",
    pages = "64--72",
    journal = "Archives of Biochemistry and Biophysics",
    issn = "0003-9861",
    publisher = "Academic Press Inc.",

    }

    Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach. / Boetsch, Cristhian; Aguayo-Villegas, Daniel R.; Gonzalez-Nilo, Fernando D.; Lisa, Teresita; Beassoni, Paola R.

    En: Archives of Biochemistry and Biophysics, Vol. 606, 15.09.2016, p. 64-72.

    Resultado de la investigación: Research - revisión exhaustivaArticle

    TY - JOUR

    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

    UR - http://www.scopus.com/inward/record.url?scp=84978634555&partnerID=8YFLogxK

    U2 - 10.1016/j.abb.2016.07.005

    DO - 10.1016/j.abb.2016.07.005

    M3 - Article

    VL - 606

    SP - 64

    EP - 72

    JO - Archives of Biochemistry and Biophysics

    T2 - Archives of Biochemistry and Biophysics

    JF - Archives of Biochemistry and Biophysics

    SN - 0003-9861

    ER -