The structure of Prp2 bound to RNA and ADP-BeF
DEAH-box ATPases
Prp2
Prp43
RNA helicases
spliceosome
Journal
Acta crystallographica. Section D, Structural biology
ISSN: 2059-7983
Titre abrégé: Acta Crystallogr D Struct Biol
Pays: United States
ID NLM: 101676043
Informations de publication
Date de publication:
01 Apr 2021
01 Apr 2021
Historique:
received:
28
08
2020
accepted:
02
02
2021
entrez:
7
4
2021
pubmed:
8
4
2021
medline:
28
10
2021
Statut:
ppublish
Résumé
Noncoding intron sequences present in precursor mRNAs need to be removed prior to translation, and they are excised via the spliceosome, a multimegadalton molecular machine composed of numerous protein and RNA components. The DEAH-box ATPase Prp2 plays a crucial role during pre-mRNA splicing as it ensures the catalytic activation of the spliceosome. Despite high structural similarity to other spliceosomal DEAH-box helicases, Prp2 does not seem to function as an RNA helicase, but rather as an RNA-dependent ribonucleoprotein particle-modifying ATPase. Recent crystal structures of the spliceosomal DEAH-box ATPases Prp43 and Prp22, as well as of the related RNA helicase MLE, in complex with RNA have contributed to a better understanding of how RNA binding and processivity might be achieved in this helicase family. In order to shed light onto the divergent manner of function of Prp2, an N-terminally truncated construct of Chaetomium thermophilum Prp2 was crystallized in the presence of ADP-BeF
Identifiants
pubmed: 33825710
pii: S2059798321001194
doi: 10.1107/S2059798321001194
pmc: PMC8025883
doi:
Substances chimiques
RNA
63231-63-0
DEAD-box RNA Helicases
EC 3.6.4.13
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
496-509Subventions
Organisme : Deutsche Forschungsgemeinschaft
ID : TP A02 A16
Organisme : Deutsche Forschungsgemeinschaft
ID : EXC 2067/1-390729940
Informations de copyright
open access.
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