6fa5 | pdb_00006fa5

CRYSTAL STRUCTURE OF THE DEAH-BOX HELICASE PRP2 IN COMPLEX WITH ADP

spinqualitylabelsall models 6fa5, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fa5 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MG, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Crystal structure of the spliceosomal DEAH-box ATPase Prp2.,Schmitt A, Hamann F, Neumann P, Ficner R Acta Crystallogr D Struct Biol. 2018 Jul 1;74(Pt 7):643-654. doi:, 10.1107/S2059798318006356. Epub 2018 Jun 8. PMID:29968674 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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