The structure of Prp2 bound to RNA and ADP-BeF


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
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

496-509

Subventions

Organisme : Deutsche Forschungsgemeinschaft
ID : TP A02 A16
Organisme : Deutsche Forschungsgemeinschaft
ID : EXC 2067/1-390729940

Informations de copyright

open access.

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Auteurs

Florian Hamann (F)

Department of Molecular Structural Biology, Institute of Microbiology and Genetics, Göttingen Center for Molecular Biosciences (GZMB), Georg-August-University Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany.

Lars C Zimmerningkat (LC)

Department of Molecular Structural Biology, Institute of Microbiology and Genetics, Göttingen Center for Molecular Biosciences (GZMB), Georg-August-University Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany.

Robert A Becker (RA)

Theoretical Physics and Center for Biophysics, Saarland University, Saarbrücken, Germany.

Tim B Garbers (TB)

Department of Molecular Structural Biology, Institute of Microbiology and Genetics, Göttingen Center for Molecular Biosciences (GZMB), Georg-August-University Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany.

Piotr Neumann (P)

Department of Molecular Structural Biology, Institute of Microbiology and Genetics, Göttingen Center for Molecular Biosciences (GZMB), Georg-August-University Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany.

Jochen S Hub (JS)

Theoretical Physics and Center for Biophysics, Saarland University, Saarbrücken, Germany.

Ralf Ficner (R)

Department of Molecular Structural Biology, Institute of Microbiology and Genetics, Göttingen Center for Molecular Biosciences (GZMB), Georg-August-University Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany.

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Classifications MeSH