Production and crystallization of alpha-phosphoglucomutase from Lactococcus lactis

Margarida Archer Frazao; Ana Rute Neves

doi:10.1107/S1744309112032629

Production and crystallization of alpha-phosphoglucomutase from Lactococcus lactis

Margarida Archer Frazao, Ana Rute Neves

Instituto de Tecnologia Química e Biológica António Xavier (ITQB)

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

alpha-Phosphoglucomutase (alpha-PGM) is an enzyme that is essential for the growth of Lactococcus lactis. The enzyme links bacterial anabolism with sugar utilization through glycolysis by catalyzing the reversible interconversion of glucose 6-phosphate and alpha-glucose 1-phosphate. The gene encoding alpha-PGM was cloned and overexpressed in L. lactis. The purified protein was functionally active and was crystallized with ammonium sulfate as a precipitant using vapour-diffusion and seeding techniques. Optimized crystals diffracted to 1.5 angstrom resolution at a synchrotron source.

Original language	Unknown
Pages (from-to)	1113-1115
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	68
Issue number	NA
DOIs	https://doi.org/10.1107/S1744309112032629
Publication status	Published - 1 Jan 2012

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10.1107/S1744309112032629

Cite this

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title = "Production and crystallization of alpha-phosphoglucomutase from Lactococcus lactis",

abstract = "alpha-Phosphoglucomutase (alpha-PGM) is an enzyme that is essential for the growth of Lactococcus lactis. The enzyme links bacterial anabolism with sugar utilization through glycolysis by catalyzing the reversible interconversion of glucose 6-phosphate and alpha-glucose 1-phosphate. The gene encoding alpha-PGM was cloned and overexpressed in L. lactis. The purified protein was functionally active and was crystallized with ammonium sulfate as a precipitant using vapour-diffusion and seeding techniques. Optimized crystals diffracted to 1.5 angstrom resolution at a synchrotron source.",

keywords = "Lactococcus lactis, a-phosphoglucomutase",

author = "Frazao, {Margarida Archer} and Neves, {Ana Rute}",

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doi = "10.1107/S1744309112032629",

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journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

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T1 - Production and crystallization of alpha-phosphoglucomutase from Lactococcus lactis

AU - Frazao, Margarida Archer

AU - Neves, Ana Rute

PY - 2012/1/1

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N2 - alpha-Phosphoglucomutase (alpha-PGM) is an enzyme that is essential for the growth of Lactococcus lactis. The enzyme links bacterial anabolism with sugar utilization through glycolysis by catalyzing the reversible interconversion of glucose 6-phosphate and alpha-glucose 1-phosphate. The gene encoding alpha-PGM was cloned and overexpressed in L. lactis. The purified protein was functionally active and was crystallized with ammonium sulfate as a precipitant using vapour-diffusion and seeding techniques. Optimized crystals diffracted to 1.5 angstrom resolution at a synchrotron source.

AB - alpha-Phosphoglucomutase (alpha-PGM) is an enzyme that is essential for the growth of Lactococcus lactis. The enzyme links bacterial anabolism with sugar utilization through glycolysis by catalyzing the reversible interconversion of glucose 6-phosphate and alpha-glucose 1-phosphate. The gene encoding alpha-PGM was cloned and overexpressed in L. lactis. The purified protein was functionally active and was crystallized with ammonium sulfate as a precipitant using vapour-diffusion and seeding techniques. Optimized crystals diffracted to 1.5 angstrom resolution at a synchrotron source.

KW - Lactococcus lactis

KW - a-phosphoglucomutase

U2 - 10.1107/S1744309112032629

DO - 10.1107/S1744309112032629

M3 - Article

SN - 1744-3091

VL - 68

SP - 1113

EP - 1115

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - NA

ER -