Effector regulation in a monomeric enzyme

被引：4

作者：

Ludwig, ML

Matthews, RG

机构：

[1] Univ Michigan, Dept Biol Chem, Ann Arbor, MI 48105 USA

[2] Univ Michigan, Div Biophys Res, Ann Arbor, MI 48105 USA

来源：

NATURE STRUCTURAL BIOLOGY | 2002年 / 9卷 / 04期

关键词：

D O I：

10.1038/nsb0402-236

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 monomeric B-12-dependent ribonucleotide reductase from L. leichmannii has the central 10-stranded alpha/beta-barrel found in all ribonucleotide reductases but incorporates two distinctive structural features, a novel cobalamin-binding fold and an insert forming part of a specificity control site that mimics the allosteric site found in the oligomeric di-iron dependent reductases.

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页码：236 / 238

页数：4

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