Ternary Structure of T4DAM with AdoHcy and DNA

File:1q0t.gif


PDB ID 1q0t

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, resolution 3.1Å
Ligands: and
Gene: DAM (Bacteriophage T4)
Activity: Site-specific DNA-methyltransferase (adenine-specific), with EC number 2.1.1.72
Coordinates: save as pdb, mmCIF, xml



OverviewOverview

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 beta-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.

About this StructureAbout this Structure

1Q0T is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the bacteriophage T4 DNA adenine methyltransferase., Yang Z, Horton JR, Zhou L, Zhang XJ, Dong A, Zhang X, Schlagman SL, Kossykh V, Hattman S, Cheng X, Nat Struct Biol. 2003 Oct;10(10):849-55. Epub 2003 Aug 24. PMID:12937411

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