Homology modelling of the DNA 5mC methyltransferase M.BssHII. Is permutation of functional subdomains common to all subfamilies of DNA methyltransferases?
This work presents a full tertiary model of the M.BssHII methyltransferase (MTase) complexed with substrate DNA and cofactor S-adenosyl-L-methionine, built by homology modelling based on previously solved complete structures of DNA MTases M.HaeIII and M. HhaI. M.BssHII and the template proteins show high sequence similarity, which indicates that they are evolutionary related. However, they are topologically different: M.BssHII is a circularly permuted variant of template MTases (Xu et al. Nucleic Acids Res 1997;25:3991). The model developed in this work will be a good starting point and valuable help in designing mutagenesis experiments to better understand the biological function of methyltransferases and the process of domain swapping.
Bujnicki
J M
JM
Molecular Biology Research Program, Henry Ford Health System, One Ford Place, Suite 5D, 48202, Detroit, MI, USA. iamb@bioinfo.pl
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D015257:DNA-Cytosine Methylases / Q000737:chemistry* / Q000378:metabolism; D016208:Databases, Factual; D019143:Evolution, Molecular; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D012436:S-Adenosylmethionine / Q000737:chemistry* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D012984:Software
D001426:Bacterial Proteins; D012436:S-Adenosylmethionine; D004247:DNA; C094508:BSSHII methyltransferase; C037664:DNA modification methylase HhaI; D015257:DNA-Cytosine Methylases; C027823:Cytosine 5-methyltransferase