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Crystal structure of the spliceosomal DEAH-box ATPase Prp2.

ABSTRACT: The DEAH-box ATPase Prp2 plays a key role in the activation of the spliceosome as it promotes the transition from the Bact to the catalytically active B* spliceosome. Here, four crystal structures of Prp2 are reported: one of the nucleotide-free state and three different structures of the ADP-bound state. The overall conformation of the helicase core, formed by two RecA-like domains, does not differ significantly between the ADP-bound and the nucleotide-free states. However, intrinsic flexibility of Prp2 is observed, varying the position of the C-terminal domains with respect to the RecA domains. Additionally, in one of the structures a unique ADP conformation is found which has not been observed in any other DEAH-box, DEAD-box or NS3/NPH-II helicase.

SUBMITTER: Schmitt A

PROVIDER: S-EPMC6038383 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature

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Crystal structure of the spliceosomal DEAH-box ATPase Prp2.

Schmitt Andreas A Hamann Florian F Neumann Piotr P Ficner Ralf R

Acta crystallographica. Section D, Structural biology 20180608 Pt 7

The DEAH-box ATPase Prp2 plays a key role in the activation of the spliceosome as it promotes the transition from the Bact to the catalytically active B* spliceosome. Here, four crystal structures of Prp2 are reported: one of the nucleotide-free state and three different structures of the ADP-bound state. The overall conformation of the helicase core, formed by two RecA-like domains, does not differ significantly between the ADP-bound and the nucleotide-free states. However, intrinsic ...[more]

PMID: 29968674

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