6FA9
CRYSTAL STRUCTURE OF THE DEAH-BOX HELICASE PRP2
Summary for 6FA9
| Entry DOI | 10.2210/pdb6fa9/pdb |
| Descriptor | Putative mRNA splicing factor, SULFATE ION (3 entities in total) |
| Functional Keywords | splicing, atpase, helicase, g-patch, hydrolase |
| Biological source | Chaetomium thermophilum |
| Total number of polymer chains | 1 |
| Total formula weight | 73112.71 |
| Authors | Schmitt, A.,Hamann, F.,Neumann, P.,Ficner, R. (deposition date: 2017-12-15, release date: 2018-07-11, Last modification date: 2024-01-17) |
| Primary citation | Schmitt, A.,Hamann, F.,Neumann, P.,Ficner, R. Crystal structure of the spliceosomal DEAH-box ATPase Prp2. Acta Crystallogr D Struct Biol, 74:643-654, 2018 Cited by 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 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. PubMed: 29968674DOI: 10.1107/S2059798318006356 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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