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Crystal structure of the spliceosomal DEAH‐box ATPase Prp2
Author(s) -
Schmitt Andreas,
Hamann Florian,
Neumann Piotr,
Ficner Ralf
Publication year - 2018
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798318006356
Subject(s) - helicase , dead box , nucleotide , atpase , spliceosome , crystallography , rna helicase a , biology , chemistry , biophysics , rna , genetics , rna splicing , biochemistry , enzyme , gene
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.