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Structure of the bacteriophage T4 DNA adenine methyltransferase.
- Source :
-
Nature Structural Biology . Sep2003, Vol. 10 Issue 10, p849-855. 7p. - Publication Year :
- 2003
-
Abstract
- DNA-adenine methylation at certain GATC sites plays a pivotal role in bacterial and phage gene expression as well as bacterial virulence. We report here the crystal structures of the bacteriophage T4Dam DNA adenine methyltransferase (MTase) in a binary complex with the methyl-donor product S-adenosyl-L-homocysteine (AdoHcy) and in a ternary complex with a synthetic 12-bp DNA duplex and AdoHcy. T4Dam contains two domains: a seven-stranded catalytic domain that harbors the binding site for AdoHcy and a DNA binding domain consisting of a five-helix bundle and a ß-hairpin that is conserved in the family of GATC-related MTase orthologs. Unexpectedly, the sequence-specific T4Dam bound to DNA in a nonspecific mode that contained two Dam monomers per synthetic duplex, even though the DNA contains a single GATC site. The ternary structure provides a rare snapshot of an enzyme poised for linear diffusion along the DNA. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 10728368
- Volume :
- 10
- Issue :
- 10
- Database :
- Academic Search Index
- Journal :
- Nature Structural Biology
- Publication Type :
- Academic Journal
- Accession number :
- 10912426
- Full Text :
- https://doi.org/10.1038/nsb973