A novel ADP- and zinc-binding fold from function-directed in vitro evolution.
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.
Lo Surdo
Paola
P
Istituto di Ricerche di Biologia Molecolare (IRBM), Via Pontina Km 30.600, 00040 Pomezia, Roma, Italy. paola_losurdo@merck.com
Walsh
Martin A
MA
Sollazzo
Maurizio
M
D000244:Adenosine Diphosphate / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D018360:Crystallography, X-Ray; D019020:Directed Molecular Evolution / Q000379:methods*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D015032:Zinc / Q000378:metabolism*
D011506:Proteins; D012333:RNA, Messenger; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D015032:Zinc