2XZL

Upf1-RNA complex

Summary for 2XZL

• Entry DOI: 10.2210/pdb2xzl/pdb
• Descriptor: ATP-DEPENDENT HELICASE NAM7, 5- R(*UP*UP*UP*UP*UP*UP*UP*UP*U) -3, ZINC ION, ... (8 entities in total)
• Functional Keywords: hydrolase-rna complex, nmd, rna degradation, allosteric regulation, hydrolase/rna
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Cytoplasm: P30771
• Total number of polymer chains: 2
• Total formula weight: 96317.65

Authors

Chakrabarti, S.,Jayachandran, U.,Bonneau, F.,Fiorini, F.,Basquin, C.,Domcke, S.,Le Hir, H.,Conti, E. (deposition date: 2010-11-26, release date: 2011-03-30, Last modification date: 2023-12-20)

Primary citation

Chakrabarti, S.,Jayachandran, U.,Bonneau, F.,Fiorini, F.,Basquin, C.,Domcke, S.,Le Hir, H.,Conti, E.
Molecular Mechanisms for the RNA-Dependent ATPase Activity of Upf1 and its Regulation by Upf2.
Mol.Cell, 41:693-, 2011

PubMed Abstract: Upf1 is a crucial factor in nonsense-mediated mRNA decay, the eukaryotic surveillance pathway that degrades mRNAs containing premature stop codons. The essential RNA-dependent ATPase activity of Upf1 is triggered by the formation of the surveillance complex with Upf2-Upf3. We report crystal structures of Upf1 in the presence and absence of the CH domain, captured in the transition state with ADP:AlF₄⁻ and RNA. In isolation, Upf1 clamps onto the RNA, enclosing it in a channel formed by both the catalytic and regulatory domains. Upon binding to Upf2, the regulatory CH domain of Upf1 undergoes a large conformational change, causing the catalytic helicase domain to bind RNA less extensively and triggering its helicase activity. Formation of the surveillance complex thus modifies the RNA binding properties and the catalytic activity of Upf1, causing it to switch from an RNA-clamping mode to an RNA-unwinding mode.

PubMed: 21419344
DOI: 10.1016/J.MOLCEL.2011.02.010

Experimental method

X-RAY DIFFRACTION (2.4 Å)