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2.1.1.37: DNA (cytosine-5-)-methyltransferase

This is an abbreviated version!
For detailed information about DNA (cytosine-5-)-methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.37

Reaction

S-adenosyl-L-methionine
+
DNA containing cytosine
=
S-adenosyl-L-homocysteine
+
DNA containing 5-methylcytosine

Synonyms

5-cytosine DNA methyltransferase, C5 MTase, C5-MTase, CG recognizing DNA methyltransferase SssI, CMT1, CMT3, cytosine 5-methyltransferase, cytosine carbon 5 DNA methyltransferase, cytosine DNA methylase, cytosine DNA methyltransferase, cytosine DNA MTase, cytosine-5 methyltransferase, cytosine-specific DNA methyltransferase, DCM, DCMT, deoxyribonucleate methylase, deoxyribonucleate methyltransferase, deoxyribonucleic (cytosine-5-)-methyltransferase, deoxyribonucleic acid (cytosine-5-)-methyltransferase, deoxyribonucleic acid methylase, deoxyribonucleic acid methyltransferase, deoxyribonucleic acid modification methylase, deoxyribonucleic methylase, DMT1, DNA (cytosine-5) methyltransferase, DNA (cytosine-5)-methyltransferase 1, DNA (cytosine-5)-methyltransferase 2, DNA (cytosine-5)-methyltransferase 3A, DNA (cytosine-5)-methyltransferase 3B, DNA (cytosine-5-)-methyltransferase 3A, DNA (cytosine-C5) methyltransferase, DNA 5-cytosine methylase, DNA cytosine C(5)-methyltransferase, DNA cytosine c5 methylase, DNA cytosine methylase, DNA cytosine methyltransferase, DNA cytosine-5 methyltransferase 1, DNA cytosine-5-methyltransferase 1, DNA cytosine-5-methyltransferase 3A, DNA cytosine-5-methyltransferase 3B, DNA methylase, DNA methyltransferase, DNA methyltransferase 1, DNA methyltransferase 3a, DNA methyltransferase-1, DNA MTase, DNA transmethylase, DNA-cytosine 5-methylase, DNA-cytosine methyltransferase, DNA-methyltransferase, DNMT, Dnmt1, Dnmt1 DNA-(cytosine-C5)-methyltransferase, DNMT1 methyltransferase, Dnmt1o, Dnmt2, Dnmt3, Dnmt3a, DNMT3B, DNMT3b2, DNMTB, DRM1/2, EC 2.1.1.73, EcoRI methylase, EcoRII DNA-cytosine methylase, EhMeth, hDNMT1, hhaIM, HpaII, M.BssHII, M.BsuRIa, M.BsuRIb, M.EcoHK31l, M.HhaI, M.HhaIII, M.MpeI, M.MspI, M.SsoII, M.Ssp6803I, M.SssI, MarII, MET1, MET1B, methylphosphotriester-DNA methyltransferase, methyltransferase, deoxyribonucleate, More, MspI DNA methyltransferase, MYPE4940, NSUN2, Nt-DRM1, SinI DNA methyltransferase, SsoII, ssoIIM, SSSI, sssIM, ssssIM, type II DNA methylase, Z2389, Zmt3

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.37 DNA (cytosine-5-)-methyltransferase

Crystallization

Crystallization on EC 2.1.1.37 - DNA (cytosine-5-)-methyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the cytosine-5-methyltransferase EhMeth at a resolution of 2.15 A is presented in complex with its reaction product S-adenosyl-L-homocysteine. In contrast to the human DNMT2 structure, the active site loop (residues 80-100) of EhMeth is well defined and clearly forms an alpha-helix
-
crystal structures of HhaI methyltransferase complexed with cognate unmethylated or methylated DNA together with S-adenosyl-L-homocysteine
-
molecular dynamics simulations. The free energy profiles for the flipping of target cytosine into the enzyme active site support the major groove base eversion pathway. The closed state of enzyme increases the free energy barrier, whereas the open state reduces it. The interactions of the key loop residues of protein with cognate DNA alter the protein motions, and modulation of protein fluctuations relates to the closed catalytic complex formation. Methylation of cytosine in the active site of the closed complex destabilizes the interactions of catalytic loop residues with cognate DNA and reduces the stability of the closed state
structure-based model of the M.HhaI-DNA-cofactor complex. Residues Gln82, Tyr254 and Asn304 are in close proximity and thus might sterically interfere with the extended transferable side chains
small-angle X-ray scattering reveals two distinct protein domains of unequal size. The larger domain matches the crystallographic structure of DNA methyltransferase HhaI, and the cleft in this domain is occupied by DNA in the model. Homology modeling represents the N-terminal region either as a flexible chain of dummy residues or as a rigid structure of a homologous protein connected to the methyltransferase domain by a short flexible linker. Both models demonstrate high mobility of the N-terminal region