2LUP
RDC refined solution structure of double-stranded RNA binding domain of S. cerevisiae RNase III (rnt1p) in complex with the terminal RNA hairpin of snr47 precursor
Summary for 2LUP
| Entry DOI | 10.2210/pdb2lup/pdb |
| Related | 1T4L 2LUQ |
| NMR Information | BMRB: 18534 |
| Descriptor | RNA (32-MER), Ribonuclease 3 (2 entities in total) |
| Functional Keywords | dsrbd, rnt1p, snr47, double strand rna binding, rna binding protein-rna complex, rna binding protein/rna |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 20127.53 |
| Authors | Wang, Z.,Feigon, J. (deposition date: 2012-06-19, release date: 2012-07-04, Last modification date: 2024-05-15) |
| 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 Cited by 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: 21742266DOI: 10.1016/j.str.2011.03.022 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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