3KX2

Crystal structure of Prp43p in complex with ADP

Summary for 3KX2

• Entry DOI: 10.2210/pdb3kx2/pdb
• Descriptor: Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: rec-a domains, ob fold, winged-helix domain, atp-binding, mrna processing, mrna splicing, nucleotide-binding, hydrolase
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Nucleus: P53131
• Total number of polymer chains: 2
• Total formula weight: 176268.51

Authors

Nielsen, K.H.,Andersen, G.R.,He, Y. (deposition date: 2009-12-02, release date: 2010-01-26, Last modification date: 2024-03-20)

Primary citation

He, Y.,Andersen, G.R.,Nielsen, K.H.
Structural basis for the function of DEAH helicases
Embo Rep., 11:180-186, 2010

PubMed Abstract: DEAH helicases participate in pre-messenger RNA splicing and ribosome biogenesis. The structure of yeast Prp43p-ADP reveals the homology of DEAH helicases to DNA helicases and the presence of an oligonucleotide-binding motif. A beta-hairpin from the second RecA domain is wedged between two carboxy-terminal domains and blocks access to the occluded RNA binding site formed by the RecA domains and a C-terminal domain. ATP binding and hydrolysis are likely to induce conformational changes in the hairpin that are important for RNA unwinding or ribonucleoprotein remodelling. The structure of Prp43p provides the framework for functional and genetic analysis of all DEAH helicases.

PubMed: 20168331
DOI: 10.1038/embor.2010.11

Experimental method

X-RAY DIFFRACTION (2.2 Å)