Structural studies of EcoRII methylase: exploring similarities among methylases.
EcoRII methyltransferase (M.EcoRII) is a cytosine-C5 DNA methylating enzyme. A model of its three-dimensional structure is proposed on the basis of homology modeling. Crystal structures of two members of the same family of enzymes, HaeIII and HhaI methyltransferases (M.HaeIII and M.HhaI respectively), were used as template molecules. Molecular dynamics was used to ensure sampling of conformationally stable structures. The final model has good geometry. The DNA and cofactor binding residues are in expected positions and form proper interactions. M.EcoRII is 147 amino acids longer than the template molecules, and hence the model contains several loops that are significantly longer than those in M.HaeIII and M.HhaI. The model provides a framework for interpretation and designing site-directed mutants that have a potential to improve crystallization experiments of this enzyme, and possibly other similar enzymes.
Schroeder
S G
SG
Biochemistry Department, University of Missouri-Columbia 65211, USA.
Samudzi
C T
CT
D000595:Amino Acid Sequence; D001665:Binding Sites; D003198:Computer Simulation; D017124:Conserved Sequence; D003460:Crystallization; D015257:DNA-Cytosine Methylases / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D012984:Software; D013329:Structure-Activity Relationship
C029528:DNA modification methylase EcoRII; C037664:DNA modification methylase HhaI; D015257:DNA-Cytosine Methylases; C027823:Cytosine 5-methyltransferase