THE 3-DIMENSIONAL STRUCTURE OF GLUTATHIONE-REDUCTASE FROM ESCHERICHIA-COLI AT 3.0 A RESOLUTION

被引：29

作者：

ERMLER, U ^{[1
]}

SCHULZ, GE ^{[1
]}

机构：

[1] UNIV FREIBURG,INST ORGAN CHEM & BIOCHEM,ALBERSTR 21,W-7800 FREIBURG,GERMANY

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1991年 / 9卷 / 03期

关键词：

GLUTATHIONE REDUCTASE; X-RAY ANALYSIS; MOLECULAR REPLACEMENT; SITE-DIRECTED MUTAGENESIS;

D O I：

10.1002/prot.340090303

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：

The structure of glutathione reductase from Escherichia coli has been solved at 3 angstrom resolution using multiple isomorphous replacement, solvent flattening, and molecular replacement on the basis of the homologous (53% identical residues) and structurally well-established human enzyme. The structures of both enzyme species agree with each other in a global way; there is no domain rearrangement In detail, clear structural differences can be observed. The structure analysis of the E. coli enzyme was tackled in order to understand site-directed mutants, the most spectacular of which changed the cofactor specificity of this enzyme from NADP to NAD (Scrutton et al., 1990, Nature 343:38-43).

引用

页码：174 / 179

页数：6

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