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J Biol Chem. 2009 Aug 21;284(34):22690-6. doi: 10.1074/jbc.M109.015966. Epub 2009 Jun 4.

Coupling sequence-specific recognition to DNA modification.

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1
Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, USA.

Abstract

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 substrate binding and critically, enzyme turnover, will have broad application to enzyme specificity and drug design for this medically relevant class of enzymes.

PMID:
19497854
PMCID:
PMC2755677
DOI:
10.1074/jbc.M109.015966
[Indexed for MEDLINE]
Free PMC Article
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