Structural highlights
Function
MTH1_HAEPH This methylase recognizes the double-stranded sequence GCGC, causes specific methylation on C-2 on both strands, and protects the DNA from cleavage by the HhaI endonuclease.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Three structures have been determined for complexes between HhaI methyltransferase (M.HhaI) and oligonucleotides containing a G:A, G:U or G:AP (AP = abasic or apurinic/apyrimidinic) mismatch at the target base pair. The mismatched adenine, uracil and abasic site are all flipped out of the DNA helix and located in the enzyme's active-site pocket, adopting the same conformation as in the flipped-out normal substrate. These results, particularly the flipped-out abasic deoxyribose sugar, provide insight into the mechanism of base flipping. If the process involves the protein pushing the base out of the helix, then the push must take place not on the base, but rather on the sugar-phosphate backbone. Thus rotation of the DNA backbone is probably the key to base flipping.
Structures of HhaI methyltransferase complexed with substrates containing mismatches at the target base.,O'Gara M, Horton JR, Roberts RJ, Cheng X Nat Struct Biol. 1998 Oct;5(10):872-7. PMID:9783745[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ O'Gara M, Horton JR, Roberts RJ, Cheng X. Structures of HhaI methyltransferase complexed with substrates containing mismatches at the target base. Nat Struct Biol. 1998 Oct;5(10):872-7. PMID:9783745 doi:http://dx.doi.org/10.1038/2312
