Bisubstrate analogues as structural tools to investigate m
RNA MTases
RNA binding
RlmJ
SAM analogue
TrmK
bisubstrate analogues
inhibitor
mA
methyltransferase
Journal
RNA biology
ISSN: 1555-8584
Titre abrégé: RNA Biol
Pays: United States
ID NLM: 101235328
Informations de publication
Date de publication:
06 2019
06 2019
Historique:
pubmed:
19
3
2019
medline:
18
12
2019
entrez:
19
3
2019
Statut:
ppublish
Résumé
RNA methyltransferases (MTases) catalyse the transfer of a methyl group to their RNA substrates using most-often S-adenosyl-L-methionine (SAM) as cofactor. Only few RNA-bound MTases structures are currently available due to the difficulties in crystallising RNA:protein complexes. The lack of complex structures results in poorly understood RNA recognition patterns and methylation reaction mechanisms. On the contrary, many cofactor-bound MTase structures are available, resulting in well-understood protein:cofactor recognition, that can guide the design of bisubstrate analogues that mimic the state at which both the substrate and the cofactor is bound. Such bisubstrate analogues were recently synthesized for proteins monomethylating the N6-atom of adenine (m
Identifiants
pubmed: 30879411
doi: 10.1080/15476286.2019.1589360
pmc: PMC6546350
doi:
Substances chimiques
Enzyme Inhibitors
0
Escherichia coli Proteins
0
N(6)-methoxyadenine
17124-24-2
Methyltransferases
EC 2.1.1.-
RlmJ protein, E coli
EC 2.1.1.-
Adenine
JAC85A2161
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
798-808Références
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