Crystal structure of the Hhal DNA methyltransferase complexed with S-adenosyl-l-methionine

Xiaodong Cheng, Sanjay Kumar, Janos Posfai, James W. Pflugrath, Richard J. Roberts

Research output: Contribution to journalArticlepeer-review

371 Scopus citations

Abstract

The first three-dimensional structure of a DNA methyltransferase is presented. The crystal structure of the DNA (cytosine-5)-methyltransferase, M.Hhal (recognition sequence: GCGC), complexed with S-adenosyl-l-methionine has been determined and refined at 2.5 Å resolution. The core of the structure is dominated by sequence motifs conserved among all DNA (cytosine-5)-methyltransferases, and these are responsible for cofactor binding and methyltransferase function.

Original languageEnglish (US)
Pages (from-to)299-307
Number of pages9
JournalCell
Volume74
Issue number2
DOIs
StatePublished - Jul 30 1993
Externally publishedYes

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology

Fingerprint

Dive into the research topics of 'Crystal structure of the Hhal DNA methyltransferase complexed with S-adenosyl-l-methionine'. Together they form a unique fingerprint.

Cite this