Ontology highlight
ABSTRACT:
SUBMITTER: Bhabha G
PROVIDER: S-EPMC3151171 | biostudies-literature | 2011 Apr
REPOSITORIES: biostudies-literature
Bhabha Gira G Lee Jeeyeon J Ekiert Damian C DC Gam Jongsik J Wilson Ian A IA Dyson H Jane HJ Benkovic Stephen J SJ Wright Peter E PE
Science (New York, N.Y.) 20110401 6026
Conformational dynamics play a key role in enzyme catalysis. Although protein motions have clear implications for ligand flux, a role for dynamics in the chemical step of enzyme catalysis has not been clearly established. We generated a mutant of Escherichia coli dihydrofolate reductase that abrogates millisecond-time-scale fluctuations in the enzyme active site without perturbing its structural and electrostatic preorganization. This dynamic knockout severely impairs hydride transfer. Thus, we ...[more]