2LBS

Solution structure of double-stranded RNA binding domain of S. cerevisiae RNase III (Rnt1p) in complex with AAGU tetraloop hairpin

Summary for 2LBS

• Entry DOI: 10.2210/pdb2lbs/pdb
• Related: 1T4L
• NMR Information: BMRB: 17574
• Descriptor: RNA (32-MER), Ribonuclease 3 (2 entities in total)
• Functional Keywords: dsrbd, aagu tetraloop, hydrolase-rna complex, hydrolase/rna
• Biological source: Saccharomyces cerevisiae (yeast)
• Total number of polymer chains: 2
• Total formula weight: 20104.49

Authors

Wang, Z.,Hartman, E.,Roy, K.,Chanfreau, G.,Feigon, J. (deposition date: 2011-04-06, release date: 2011-08-31, Last modification date: 2024-05-01)

Primary citation

Wang, Z.,Hartman, E.,Roy, K.,Chanfreau, G.,Feigon, J.
Structure of a Yeast RNase III dsRBD Complex with a Noncanonical RNA Substrate Provides New Insights into Binding Specificity of dsRBDs.
Structure, 19:999-1010, 2011

PubMed Abstract: dsRBDs often bind dsRNAs with some specificity, yet the basis for this is poorly understood. Rnt1p, the major RNase III in Saccharomyces cerevisiae, cleaves RNA substrates containing hairpins capped by A/uGNN tetraloops, using its dsRBD to recognize a conserved tetraloop fold. However, the identification of a Rnt1p substrate with an AAGU tetraloop raised the question of whether Rnt1p binds to this noncanonical substrate differently than to A/uGNN tetraloops. The solution structure of Rnt1p dsRBD bound to an AAGU-capped hairpin reveals that the tetraloop undergoes a structural rearrangement upon binding to Rnt1p dsRBD to adopt a backbone conformation that is essentially the same as the AGAA tetraloop, and indicates that a conserved recognition mode is used for all Rnt1p substrates. Comparison of free and RNA-bound Rnt1p dsRBD reveals that tetraloop-specific binding requires a conformational change in helix α1. Our findings provide a unified model of binding site selection by this dsRBD.

PubMed: 21742266
DOI: 10.1016/j.str.2011.03.022

Experimental method

SOLUTION NMR