A novel ADP- and zinc-binding fold from function-directed in vitro evolution

被引：48

作者：

Lo Surdo, P

Walsh, MA

Sollazzo, M

机构：

[1] Ist Ric Biol Mol, I-00040 Rome, Italy

[2] European Synchrotron Radiat Facil, MRC France, F-38043 Grenoble, France

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2004年 / 11卷 / 04期

关键词：

D O I：

10.1038/nsmb745

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：

A great challenge to biologists is to create proteins with novel folds and tailored functions. As an alternative to de novo protein design, we investigated the structure of a randomly generated protein targeted to bind ATP. The crystal structure reveals a novel alpha/beta fold bound to its ligand, representing both the first protein structure derived from in vitro evolution and the first nucleotide-binding protein stabilized by a zinc ion.

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页码：382 / 383

页数：2

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