3-DIMENSIONAL STRUCTURE OF THE FREE-RADICAL PROTEIN OF RIBONUCLEOTIDE REDUCTASE

被引：830

作者：

NORDLUND, P ^{[1
]}

SJOBERG, BM ^{[1
]}

EKLUND, H ^{[1
]}

机构：

[1] UNIV STOCKHOLM,DEPT MOLEC BIOL,S-10691 STOCKHOLM,SWEDEN

来源：

NATURE | 1990年 / 345卷 / 6276期

关键词：

D O I：

10.1038/345593a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The enzyme ribonucleotide reductase furnishes precursors for the DNA synthesis of all living cells. One of its constituents, the free radical protein, has an unusual α-helical structure. There are two iron centres that are about 25 Å apart in the dimeric molecule. Tyrosine 122, which harbours the stable free radical necessary for the activity of ribonucleotide reductase, is buried inside the protein and is located 5 Å from the closest iron atom. © 1990 Nature Publishing Group.

引用

页码：593 / 598

页数：6

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