Ontology highlight
ABSTRACT:
SUBMITTER: Estabrook RA
PROVIDER: S-EPMC2755677 | biostudies-literature | 2009 Aug
REPOSITORIES: biostudies-literature
Estabrook R August RA Nguyen Trung T TT Fera Nickolas N Reich Norbert O NO
The Journal of biological chemistry 20090604 34
Enzymes that modify DNA are faced with significant challenges in specificity for both substrate binding and catalysis. We describe how single hydrogen bonds between M.HhaI, a DNA cytosine methyltransferase, and its DNA substrate regulate the positioning of a peptide loop which is approximately 28 A away. Stopped-flow fluorescence measurements of a tryptophan inserted into the loop provide real-time observations of conformational rearrangements. These long-range interactions that correlate with s ...[more]