4OOG

Crystal structure of yeast RNase III (Rnt1p) complexed with the product of dsRNA processing

Summary for 4OOG

• Entry DOI: 10.2210/pdb4oog/pdb
• Related: 2NUG
• Descriptor: Ribonuclease 3, 34-mer RNA, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: rnase:rna complex, ribonuclease iii domain, double-stranded rna-binding domain, endoribonuclease, dsrna-specific rnase, double-stranded rna, hydrolase-rna complex, hydrolase/rna
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 4
• Total formula weight: 66549.34

Authors

Liang, Y.-H.,Ji, X. (deposition date: 2014-02-02, release date: 2014-04-16, Last modification date: 2023-09-20)

Primary citation

Liang, Y.H.,Lavoie, M.,Comeau, M.A.,Abou Elela, S.,Ji, X.
Structure of a Eukaryotic RNase III Postcleavage Complex Reveals a Double-Ruler Mechanism for Substrate Selection.
Mol.Cell, 54:431-444, 2014

PubMed Abstract: Ribonuclease III (RNase III) enzymes are a family of double-stranded RNA (dsRNA)-specific endoribonucleases required for RNA maturation and gene regulation. Prokaryotic RNase III enzymes have been well characterized, but how eukaryotic RNase IIIs work is less clear. Here, we describe the structure of the Saccharomyces cerevisiae RNase III (Rnt1p) postcleavage complex and explain why Rnt1p binds to RNA stems capped with an NGNN tetraloop. The structure shows specific interactions between a structural motif located at the end of the Rnt1p dsRNA-binding domain (dsRBD) and the guanine nucleotide in the second position of the loop. Strikingly, structural and biochemical analyses indicate that the dsRBD and N-terminal domains (NTDs) of Rnt1p function as two rulers that measure the distance between the tetraloop and the cleavage site. These findings provide a framework for understanding eukaryotic RNase IIIs.

PubMed: 24703949
DOI: 10.1016/j.molcel.2014.03.006

Experimental method

X-RAY DIFFRACTION (2.5 Å)