6FA9

Crystal structure of the spliceosomal DEAH-box ATPase Prp2.

(2018) Acta Crystallogr D Struct Biol 74: 643-654

• PubMed: 29968674 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1107/S2059798318006356
• Primary Citation of Related Structures:  
  6FA5, 6FA9, 6FAA, 6FAC


• PubMed Abstract: 
  

  The DEAH-box ATPase Prp2 plays a key role in the activation of the spliceosome as it promotes the transition from the B ^act 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.

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Organizational Affiliation: 

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