5D0U

Crystal structure of the RNA-helicase Prp43 from Chaetomium thermophilum bound to ADP

Summary for 5D0U

Entry DOI	10.2210/pdb5d0u/pdb
Descriptor	Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
Functional Keywords	spliceosome, rna-helicase, deah-box protein, dhx15, hydrolase
Biological source	Chaetomium thermophilum var. thermophilum DSM 1495
Total number of polymer chains	1
Total formula weight	82796.04
Authors	Tauchert, M.J.,Ficner, R. (deposition date: 2015-08-03, release date: 2016-02-10, Last modification date: 2024-01-10)
Primary citation	Tauchert, M.J.,Fourmann, J.B.,Christian, H.,Luhrmann, R.,Ficner, R. Structural and functional analysis of the RNA helicase Prp43 from the thermophilic eukaryote Chaetomium thermophilum. Acta Crystallogr.,Sect.F, 72:112-120, 2016 Cited by PubMed Abstract: RNA helicases are indispensable for all organisms in each domain of life and have implications in numerous cellular processes. The DEAH-box RNA helicase Prp43 is involved in pre-mRNA splicing as well as rRNA maturation. Here, the crystal structure of Chaetomium thermophilum Prp43 at 2.9 Å resolution is revealed. Furthermore, it is demonstrated that Prp43 from C. thermophilum is capable of functionally replacing its orthologue from Saccharomyces cerevisiae in spliceosomal disassembly assays. PubMed: 26841761 DOI: 10.1107/S2053230X15024498 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.919 Å)

Structure validation