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PDBsum entry 5a7z
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PDB id:
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Transferase
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Title:
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Crystal structure of sulfolobus acidocaldarius trm10 at 2.1 angstrom resolution.
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Structure:
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tRNA (adenine(9)-n1)-methyltransferase. Chain: a. Synonym: tRNA(m1a9)-methyltransferase, tRNA(m1a9)mtase, trm10. Engineered: yes
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Source:
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Sulfolobus acidocaldarius. Organism_taxid: 2285. Atcc: 33909. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta plyss.
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Resolution:
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2.10Å
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R-factor:
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0.226
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R-free:
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0.264
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Authors:
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B.Van Laer,M.Roovers,L.Wauters,J.Kasprzak,M.Dyzma,E.Deyaert,A.Feller, J.Bujnicki,L.Droogmans,W.Versees
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Key ref:
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B.Van Laer
et al.
(2016).
Structural and functional insights into tRNA binding and adenosine N1-methylation by an archaeal Trm10 homologue.
Nucleic Acids Res,
44,
940-953.
PubMed id:
DOI:
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Date:
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10-Jul-15
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Release date:
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13-Jan-16
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PROCHECK
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Headers
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References
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Q4J894
(TRM10_SULAC) -
tRNA (adenine(9)-N1)-methyltransferase from Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
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Seq:
Struc:
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292 a.a.
250 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class:
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E.C.2.1.1.218
- tRNA (adenine(9)-N(1))-methyltransferase.
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Reaction:
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adenosine9 in tRNA + S-adenosyl-L-methionine = N1-methyladenosine9 in tRNA + S-adenosyl-L-homocysteine + H+
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adenosine(9) in tRNA
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S-adenosyl-L-methionine
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=
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N(1)-methyladenosine(9) in tRNA
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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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Nucleic Acids Res
44:940-953
(2016)
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PubMed id:
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Structural and functional insights into tRNA binding and adenosine N1-methylation by an archaeal Trm10 homologue.
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B.Van Laer,
M.Roovers,
L.Wauters,
J.M.Kasprzak,
M.Dyzma,
E.Deyaert,
R.Kumar Singh,
A.Feller,
J.M.Bujnicki,
L.Droogmans,
W.Versées.
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ABSTRACT
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Purine nucleosides on position 9 of eukaryal and archaeal tRNAs are frequently
modified in vivo by the post-transcriptional addition of a methyl group on their
N1 atom. The methyltransferase Trm10 is responsible for this modification in
both these domains of life. While certain Trm10 orthologues specifically
methylate either guanosine or adenosine at position 9 of tRNA, others have a
dual specificity. Until now structural information about this enzyme family was
only available for the catalytic SPOUT domain of Trm10 proteins that show
specificity toward guanosine. Here, we present the first crystal structure of a
full length Trm10 orthologue specific for adenosine, revealing next to the
catalytic SPOUT domain also N- and C-terminal domains. This structure hence
provides crucial insights in the tRNA binding mechanism of this unique monomeric
family of SPOUT methyltransferases. Moreover, structural comparison of this
adenosine-specific Trm10 orthologue with guanosine-specific Trm10 orthologues
suggests that the N1 methylation of adenosine relies on additional catalytic
residues.
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Links
