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Acta Crystallogr F Struct Biol Commun. 2016 May;72(Pt 5):409-16. doi: 10.1107/S2053230X16006038. Epub 2016 Apr 22.

Structural analysis of the spliceosomal RNA helicase Prp28 from the thermophilic eukaryote Chaetomium thermophilum.

Author information

1
Department of Molecular Structural Biology, Institute for Microbiology and Genetics, GZMB, Georg-August-University Göttingen, Justus-von-Liebig Weg 11, 37077 Göttingen, Germany.

Abstract

Prp28 (pre-mRNA-splicing ATP-dependent RNA helicase 28) is a spliceosomal DEAD-box helicase which is involved in two steps of spliceosome assembly. It is required for the formation of commitment complex 2 in an ATP-independent manner as well as for the formation of the pre-catalytic spliceosome, which in contrast is ATP-dependent. During the latter step, Prp28 is crucial for the integration of the U4/U6·U5 tri-snRNP since it displaces the U1 snRNP and allows the U6 snRNP to base-pair with the 5'-splice site. Here, the crystal structure of Prp28 from the thermophilic fungus Chaetomium thermophilum is reported at 3.2 Å resolution and is compared with the available structures of homologues.

KEYWORDS:

DDX23; DEAD-box protein; RNA helicase; U5-100kD; spliceosome

PMID:
27139834
PMCID:
PMC4854570
DOI:
10.1107/S2053230X16006038
[Indexed for MEDLINE]
Free PMC Article

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