A Completely <i>De Novo</i> ATPase from Combinatorial Protein Design
Michael S. Wang, Michael H. Hecht
Abstract
Our understanding of biological chemistry is shaped by the observation that all life comes from other life—as Pasteur put it, omne vivum ex vivo. A key step in expanding our biochemical vocabulary is to recapitulate biogenic catalysis using non-natural sequences that did not arise from common ancestry. Here we describe an enzyme designed completely de novo that hydrolyzes ATP. This protein was designed to lack β-sheet structure and is competitively inhibited by magnesium, two traits that are unlike natural ATPases.
Topics & Concepts
ChemistryATPaseProtein designStereochemistryComputational biologyBiochemistryEnzymeProtein structureBiologyATP Synthase and ATPases ResearchBiochemical and Molecular ResearchProtein Structure and Dynamics