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PDBsum entry 4n4a
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PDB id:
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Transferase
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Title:
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Cystal structure of cap-specific mRNA (nucleoside-2'-o-)- methyltransferase 1
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Structure:
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Cap-specific mRNA (nucleoside-2'-o-)-methyltransferase 1. Chain: a. Synonym: cap1 2'o-ribose methyltransferase 1, mtr1, hmtr1, ftsj methyltransferase domain-containing protein 2, interferon-stimulated gene 95 kda protein, isg95. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ftsjd2, kiaa0082, mtr1. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.35Å
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R-factor:
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0.156
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R-free:
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0.196
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Authors:
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M.Smietanski,M.Werener,E.Purta,K.H.Kaminska,J.Stepinski, E.Darzynkiewicz,M.Nowotny,J.M.Bujnicki
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Key ref:
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M.Smietanski
et al.
(2014).
Structural analysis of human 2'-O-ribose methyltransferases involved in mRNA cap structure formation.
Nat Commun,
5,
3004.
PubMed id:
DOI:
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Date:
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08-Oct-13
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Release date:
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22-Jan-14
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PROCHECK
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Headers
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References
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Q8N1G2
(CMTR1_HUMAN) -
Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 from Homo sapiens
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Seq:
Struc:
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835 a.a.
398 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.2.1.1.57
- methyltransferase cap1.
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Reaction:
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a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)- (2'-O-methyl-ribonucleoside) in mRNA + S-adenosyl-L-homocysteine + H+
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5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA
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+
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S-adenosyl-L-methionine
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=
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5'-end (N(7)-methyl 5'-triphosphoguanosine)- (2'-O-methyl-ribonucleoside) in mRNA
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+
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S-adenosyl-L-homocysteine
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Nat Commun
5:3004
(2014)
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PubMed id:
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Structural analysis of human 2'-O-ribose methyltransferases involved in mRNA cap structure formation.
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M.Smietanski,
M.Werner,
E.Purta,
K.H.Kaminska,
J.Stepinski,
E.Darzynkiewicz,
M.Nowotny,
J.M.Bujnicki.
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ABSTRACT
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The 5' cap of human messenger RNA contains 2'-O-methylation of the first and
often second transcribed nucleotide that is important for its processing,
translation and stability. Human enzymes that methylate these nucleotides,
termed CMTr1 and CMTr2, respectively, have recently been identified. However,
the structures of these enzymes and their mechanisms of action remain unknown.
In the present study, we solve the crystal structures of the active CMTr1
catalytic domain in complex with a methyl group donor and a capped
oligoribonucleotide, thereby revealing the mechanism of specific recognition of
capped RNA. This mechanism differs significantly from viral enzymes, thus
providing a framework for their specific targeting. Based on the crystal
structure of CMTr1, a comparative model of the CMTr2 catalytic domain is
generated. This model, together with mutational analysis, leads to the
identification of residues involved in RNA and methyl group donor binding.
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