Quarterly Reviews of Biophysics



Review Article

Nucleoside triphosphate-binding proteins: different scaffolds to achieve phosphoryl transfer


Ingrid R. Vetter a1 and Alfred Wittinghofer a1
a1 MPI für Molekulare Physiologie, Abteilung Strukturelle Biologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany

Abstract

Nucleoside triphosphates are crucial mediators of life. The high energy phosphoanhydride bond of (usually) ATP is used to drive unfavorable chemical reactions, to fuel biological machines, and to regulate a vast number of processes via phosphorylation of proteins. GTP, in turn, is used almost exclusively for the regulation of signal transduction and transport processes, whereas the other nucleotides play a less important role, except in synthesis pathways involving sugars (UTP) and phospholipids (CTP) and as building blocks of polynucleotides such as RNA and DNA. Proteins that bind and use these nucleotides for enzymatic reaction and regulation are very diverse. Although some of them constitute the largest protein superfamilies known (e.g. protein kinases), others seem to be far less conserved in evolution.