THE ISOLATION, PURIFICATION, AND PRELIMINARY CRYSTALLOGRAPHIC CHARACTERIZATION OF UDP-GALACTOSE-4-EPIMERASE FROM ESCHERICHIA-COLI

被引：20

作者：

BAUER, AJ

RAYMENT, I

FREY, PA

HOLDEN, HM

机构：

[1] UNIV WISCONSIN,GRAD SCH,INST ENZYME RES,1710 UNIV AVE,MADISON,WI 53706

[2] UNIV WISCONSIN,COLL PSYCHOL,DEPT BIOCHEM,MADISON,WI 53706

[3] UNIV WISCONSIN,COLL LETTERS & SCI,DEPT CHEM,MADISON,WI 53706

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1991年 / 9卷 / 02期

关键词：

X-RAY CRYSTALLOGRAPHY; GALACTOSE METABOLISM; NUCLEOTIDE BINDING; NONSTEREOSPECIFIC HYDRIDE TRANSFER; PROTEIN STRUCTURE;

D O I：

10.1002/prot.340090207

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Uridine diphosphogalactose-4-epimerase from E. coli has been crystallized in a form suitable for a high-resolution X-ray crystallographic structural analysis. The enzyme complexed with a substrate analogue, uridine diphosphobenzene (UDP-benzene), crystallizes readily using polyethylene glycol 8000 as the precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)21(1) with unit cell dimensions, a = 76.3 angstrom, b = 83.1 angstrom, and c = 132.1 angstrom. Based on still setting photographs, the crystals diffract to a nominal resolution of 2.3 angstrom and are stable in the X-ray beam. The enzyme used in these experiments was produced by a new expression system and a modified purification scheme.

引用

页码：135 / 142

页数：8

共 23 条

[1]

ADAIR WL, 1973, J BIOL CHEM, V248, P4635

[2]

ADAIR WL, 1973, J BIOL CHEM, V248, P4640

[3] THE GALACTOSE-GLUCOSE CONVERSION IN ISOTOPIC WATER [J].