EzCatDB: S00637
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DB codeS00637
CATH domainDomain 13.40.50.150 : Rossmann foldCatalytic domain
E.C.2.1.1.56

CATH domainRelated DB codes (homologues)
3.40.50.150 : Rossmann foldS00639,S00262,S00261,S00291,S00412,D00075,D00076,D00079,D00080,D00082,D00083,D00823

Enzyme Name
UniProtKBKEGG

Q8SR66
Protein namemRNA cap guanine-N7 methyltransferase (EC 2.1.1.56) (mRNAmRNA (guanine-N7-)-methyltransferase
Messenger ribonucleate guanine 7-methyltransferase
Guanine-7-methyltransferase
Messenger RNA guanine 7-methyltransferase
S-Adenosyl-L-methionine:mRNA (guanine-7-N-)-methyltransferase
Synonymsguanine-N(7)-)-methyltransferase
mRNA cap methyltransferase
RefSeqNP_586153.1 (Protein)
NM_001041986.1 (DNA/RNA sequence)
PfamPF03291 (Pox_MCEL)
[Graphical view]


UniProtKB:Accession NumberQ8SR66
Entry nameMCES_ENCCU
ActivityS-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
SubunitMonomer.
Subcellular locationNucleus (By similarity).
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00019C02031C00021C02339
CompoundS-adenosyl-L-methionineG(5')pppR-RNAS-adenosyl-L-homocysteinem7G(5')pppR-RNA
Typeamino acids,amine group,nucleoside,sulfonium ionamide group,amine group,nucleic acids,nucleotideamino acids,amine group,nucleoside,sulfide groupnucleic acids,nucleotide
ChEBI67040

16680
57856

PubChem34755

439155
25246222

            
1ri1A00UnboundAnalogue:GTGBound:SAHUnbound
1ri2A00UnboundAnalogue:GTGUnboundUnbound
1ri3A00UnboundUnboundBound:SAHUnbound
1ri4A00Bound:SAMUnboundUnboundUnbound
1ri5A00UnboundUnboundUnboundUnbound
1z3cA00Analogue:SA8UnboundUnboundUnbound
2hv9A00Analogue:SFGUnboundUnboundUnbound

Active-site residues
resource
literature [6] & [8]
pdbCatalytic residues
         
1ri1A00PHE 141;TYR 145
1ri2A00PHE 141;TYR 145
1ri3A00PHE 141;TYR 145
1ri4A00PHE 141;TYR 145
1ri5A00PHE 141;TYR 145
1z3cA00PHE 141;TYR 145
2hv9A00PHE 141;TYR 145

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]p85-87
[7]p20410-20412
[8]p35908

references
[1]
PubMed ID8639642
JournalBiochemistry
Year1996
Volume35
Pages6900-10
AuthorsMao X, Shuman S
TitleVaccinia virus mRNA (guanine-7-)methyltransferase: mutational effects on cap methylation and AdoHcy-dependent photo-cross-linking of the cap to the methyl acceptor site.
[2]
PubMed ID10347220
JournalJ Biol Chem
Year1999
Volume274
Pages16553-62
AuthorsSaha N, Schwer B, Shuman S
TitleCharacterization of human, Schizosaccharomyces pombe, and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes.
[3]
PubMed ID12859184
JournalBiochemistry
Year2003
Volume42
Pages8394-402
AuthorsTakata Y, Huang Y, Komoto J, Yamada T, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F
TitleCatalytic mechanism of glycine N-methyltransferase.
Related PDB1nbh,1nbi
[4]
PubMed ID12805428
JournalJ Virol
Year2003
Volume77
Pages7300-7
AuthorsSaha N, Shuman S, Schwer B
TitleYeast-based genetic system for functional analysis of poxvirus mRNA cap methyltransferase.
[5]
PubMed ID12826405
JournalTrends Biochem Sci
Year2003
Volume28
Pages329-35
AuthorsSchubert HL, Blumenthal RM, Cheng X
TitleMany paths to methyltransfer: a chronicle of convergence.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES
PubMed ID14731396
JournalMol Cell
Year2004
Volume13
Pages77-89
AuthorsFabrega C, Hausmann S, Shen V, Shuman S, Lima CD
TitleStructure and mechanism of mRNA cap (guanine-N7) methyltransferase.
Related PDB1ri1,1ri2,1ri3,1ri4,1ri5
Related UniProtKBQ8SR66
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG
PubMed ID15760890
JournalJ Biol Chem
Year2005
Volume280
Pages20404-12
AuthorsHausmann S, Zheng S, Fabrega C, Schneller SW, Lima CD, Shuman S
TitleEncephalitozoon cuniculi mRNA cap (guanine N-7) methyltransferase: methyl acceptor specificity, inhibition BY S-adenosylmethionine analogs, and structure-guided mutational analysis.
Related PDB1z3c
Related UniProtKBQ8SR66
[8]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG
PubMed ID16971388
JournalJ Biol Chem
Year2006
Volume281
Pages35904-13
AuthorsZheng S, Hausmann S, Liu Q, Ghosh A, Schwer B, Lima CD, Shuman S
TitleMutational analysis of Encephalitozoon cuniculi mRNA cap (guanine-N7) methyltransferase, structure of the enzyme bound to sinefungin, and evidence that cap methyltransferase is the target of sinefungin's antifungal activity.
Related PDB2hv9
Related UniProtKBQ8SR66

comments
This enzyme belongs to the class I methyltransferase family.
This enzyme is closely related to glycine N-methltransferase (EC 2.1.1.20; D00075 in EzCatDb).
According to the literature [6], [7] and [8], this enzyme facilitates methyl transfer from S-adenosyl-L-methionine (AdoMet) to the substrate guanine-N7 by coordinating the donor and acceptor in an environment that optimizes substrate proximity and orientation. Moreover, the shape of the guanine binding pocket is more important than particular base edge interactions. In this enzyme, the aliphatic carbon atoms of Phe141 and Tyr145 which engage in multiple van der Waals contacts with guanosine and AdoMet are more important in the in-lime mechanism of methyl transfer, rather than polar functional groups of active-site residues (see [6] and [8]).

createdupdated
2009-04-232011-12-20


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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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