Expression, purification, crystallization and preliminary X-ray analysis of glucose-1-phosphate uridylyltransferase (GalU) from Erwinia amylovora

被引：7

作者：

Toccafondi, Mirco ^{[1
]}

Cianci, Michele ^{[2
]}

Benini, Stefano ^{[1
]}

机构：

[1] Free Univ Bolzano, Fac Sci & Technol, Lab Bioorgan Chem & Biocrystallog B2Cl, I-39100 Bolzano, Italy

[2] EMBL, D-22607 Hamburg, Germany

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2014年 / 70卷

关键词：

UDP-GLUCOSE PYROPHOSPHORYLASE; FIRE BLIGHT PATHOGEN; EXOPOLYSACCHARIDES AMYLOVORAN; BIOCHEMICAL-CHARACTERIZATION; POLYSACCHARIDE BIOSYNTHESIS; STREPTOCOCCUS-PNEUMONIAE; BIOFILM FORMATION; VIRULENCE; GENE; GALACTOSE;

D O I：

10.1107/S2053230X14016458

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Glucose-1-phosphate uridylyltransferase from Erwinia amylovora CFPB1430 was expressed as a His-tag fusion protein in Escherichia coli. After tag removal, the purified protein was crystallized from 100 mM Tris pH 8.5, 2 M ammonium sulfate, 5% ethylene glycol. Diffraction data sets were collected to a maximum resolution of 2.46 angstrom using synchrotron radiation. The crystals belonged to the hexagonal space group P6(2), with unit-cell parameters a = 80.67, b = 80.67, c = 169.18. The structure was solved by molecular replacement using the structure of the E. coli enzyme as a search model.

引用

页码：1249 / 1251

页数：3

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