Ontology highlight
ABSTRACT:
SUBMITTER: Watt ED
PROVIDER: S-EPMC1924554 | biostudies-literature | 2007 Jul
REPOSITORIES: biostudies-literature
Watt Eric D ED Shimada Hiroko H Kovrigin Evgenii L EL Loria J Patrick JP
Proceedings of the National Academy of Sciences of the United States of America 20070705 29
The ability to use conformational flexibility is a hallmark of enzyme function. Here we show that protein motions and catalytic activity in a RNase are coupled and display identical solvent isotope effects. Solution NMR relaxation experiments identify a cluster of residues, some distant from the active site, that are integral to this motion. These studies implicate a single residue, histidine-48, as the key modulator in coupling protein motion with enzyme function. Mutation of H48 to alanine res ...[more]