STRUCTURE OF TERNARY COMPLEX OF HHAI METHYLTRANSFERASE MUTANT (T250G) IN COMPLEX WITH DNA AND ADOHCY

Functional roles of the conserved threonine 250 in the target recognition domain of HhaI DNA methyltransferase.

DNA (5'-D(*TP*GP*AP*TP*AP*GP*CP*GP*CP*TP*AP*TP*C)-3')

MIEIKDKQLTGLRFIDLFAGLGGFRLALESCGAECVYSNEWDKYAQEVYEMNFGEKPEGDITQVNEKTIPDHDILCAGFP
CQAFSISGKQKGFEDSRGTLFFDIARIVREKKPKVVFMENVKNFASHDNGNTLEVVKNTMNELDYSFHAKVLNALDYGIP
QKRERIYMICFRNDLNIQNFQFPKPFELNTFVKDLLLPDSEVEHLVIDRKDLVMTNQEIEQTTPKTVRLGIVGKGGQGER
IYSTRGIAIGLSAYGGGIFAKTGGYLVNGKTRKLHPRECARVMGYPDSYKVHPSTSQAYKQFGNSVVINVLQYIAYNIGS
SLNFKPY

2.7 M ammonium sulfate 20% (w/v) glucose 50 mM sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 16K

3MHT contains the wild type HhaI methyltransferase, the same DNA sequence used and the same cofactor AdoHcy

The biological assembly is a ternary complex from HhaI Methyltransferase, a palindromic oligonucleotide, and S-adenosyl-l-homocysteine (AdoHcy)

AdoMet-dependent Methyltransferase fold protein-DNA-cofactor complex, TRANSFERASE-DNA COMPLEX