通过功能导向的体外进化获得的一种新型ADP和锌结合折叠结构。
A novel ADP- and zinc-binding fold from function-directed in vitro evolution.
作者信息
Lo Surdo Paola, Walsh Martin A, Sollazzo Maurizio
机构信息
Istituto di Ricerche di Biologia Molecolare (IRBM), Via Pontina Km 30.600, 00040 Pomezia, Roma, Italy.
出版信息
Nat Struct Mol Biol. 2004 Apr;11(4):382-3. doi: 10.1038/nsmb745. Epub 2004 Mar 14.
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.
对生物学家来说，一个巨大的挑战是创造出具有新颖折叠结构和特定功能的蛋白质。作为从头开始进行蛋白质设计的替代方法，我们研究了一种靶向结合ATP的随机生成蛋白质的结构。晶体结构揭示了一种与其配体结合的新型α/β折叠结构，它既是首个源自体外进化的蛋白质结构，也是首个由锌离子稳定的核苷酸结合蛋白。
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