3PIE

Crystal structure of the 5'->3' exoribonuclease Xrn1, E178Q mutant

Summary for 3PIE

• Entry DOI: 10.2210/pdb3pie/pdb
• Related: 3PIF
• Descriptor: 5'->3' EXORIBONUCLEASE (Xrn1) (1 entity in total)
• Functional Keywords: beta berrel, tudor domain, chromo domain, mrna turnover, rrna processing, rna binding, dna binding, hydrolase
• Biological source: Kluyveromyces lactis (Yeast); More
• Cellular location: Cytoplasm : Q6CJ09
• Total number of polymer chains: 4
• Total formula weight: 529379.25

Authors

Chang, J.H.,Xiang, S.,Tong, L. (deposition date: 2010-11-06, release date: 2011-02-09, Last modification date: 2024-02-21)

Primary citation

Chang, J.H.,Xiang, S.,Xiang, K.,Manley, J.L.,Tong, L.
Structural and biochemical studies of the 5' -> 3' exoribonuclease Xrn1.
Nat.Struct.Mol.Biol., 18:270-276, 2011

PubMed Abstract: The 5'→3' exoribonucleases (XRNs) have important functions in transcription, RNA metabolism and RNA interference. The structure of Rat1 (also known as Xrn2) showed that the two highly conserved regions of XRNs form a single, large domain that defines the active site of the enzyme. Xrn1 has a 510-residue segment after the conserved regions that is required for activity but is absent from Rat1/Xrn2. Here we report the crystal structures of Kluyveromyces lactis Xrn1 (residues 1-1,245, E178Q mutant), alone and in complex with a Mn(2+) ion in the active site. The 510-residue segment contains four domains (D1-D4), located far from the active site. Our mutagenesis and biochemical studies show that their functional importance results from their ability to stabilize the conformation of the N-terminal segment of Xrn1. These domains might also constitute a platform that interacts with protein partners of Xrn1.

PubMed: 21297639
DOI: 10.1038/nsmb.1984

Experimental method

X-RAY DIFFRACTION (2.9 Å)