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2XZO

Upf1 helicase - RNA complex

Summary for 2XZO
Entry DOI10.2210/pdb2xzo/pdb
Related2GJK 2GK6 2GK7 2IYK 2WJV 2WJY 2XZP
DescriptorREGULATOR OF NONSENSE TRANSCRIPTS 1, 5'-R(*UP*UP*UP*UP*UP*UP*UP)-3', PENTAETHYLENE GLYCOL, ... (7 entities in total)
Functional Keywordshydrolase-rna complex, nmd, rna degradation, allosteric regulation, hydrolase/rna
Biological sourceHOMO SAPIENS (HUMAN)
More
Cellular locationCytoplasm: Q92900
Total number of polymer chains2
Total formula weight73420.23
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 citationChakrabarti, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.395 Å)
Structure validation

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