8CNT
Structure of the DEAH-box helicase Prp16 in complex with ADP
Summary for 8CNT
| Entry DOI | 10.2210/pdb8cnt/pdb |
| Descriptor | Pre-mRNA splicing factor ATP-dependent RNA helicase prp16-like protein, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | deah-box helicase, hydrolase |
| Biological source | Thermochaetoides thermophila DSM 1495 |
| Total number of polymer chains | 1 |
| Total formula weight | 72265.00 |
| Authors | |
| Primary citation | Garbers, T.B.,Enders, M.,Neumann, P.,Ficner, R. Crystal structure of Prp16 in complex with ADP. Acta Crystallogr.,Sect.F, 79:200-207, 2023 Cited by PubMed Abstract: DEAH-box helicases play a crucial role in pre-mRNA splicing as they are responsible for major rearrangements of the spliceosome and are involved in various quality-ensuring steps. Prp16 is the driving force during spliceosomal catalysis, remodeling the C state into the C* state. Here, the first crystal structure of Prp16 from Chaetomium thermophilum in complex with ADP is reported at 1.9 Å resolution. Comparison with the other spliceosomal DEAH-box helicases Prp2, Prp22 and Prp43 reveals an overall identical domain architecture. The β-hairpin, which is a structural element of the RecA2 domain, exhibits a unique position, punctuating its flexibility. Analysis of cryo-EM models of spliceosomal complexes containing Prp16 reveals that these models show Prp16 in its nucleotide-free state, rendering the model presented here the first structure of Prp16 in complex with a nucleotide. PubMed: 37548918DOI: 10.1107/S2053230X23005721 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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