Summary information and primary citation
- PDB-id
- 1rc7; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- hydrolase-RNA
- Method
- X-ray (2.15 Å)
- Summary
- Crystal structure of rnase iii mutant e110k from aquifex aeolicus complexed with ds-RNA at 2.15 angstrom resolution
- Reference
- Blaszczyk J, Gan J, Tropea JE, Court DL, Waugh DS, Ji X (2004): "Noncatalytic Assembly of Ribonuclease III with Double-Stranded RNA." Structure, 12, 457-466. doi: 10.1016/j.str.2004.02.004.
- Abstract
- Ribonuclease III (RNase III) represents a family of double-stranded RNA (dsRNA) endonucleases. The simplest bacterial enzyme contains an endonuclease domain (endoND) and a dsRNA binding domain (dsRBD). RNase III can affect RNA structure and gene expression in either of two ways: as a dsRNA-processing enzyme that cleaves dsRNA, or as a dsRNA binding protein that binds but does not cleave dsRNA. We previously determined the endoND structure of Aquifex aeolicus RNase III (Aa-RNase III) and modeled a catalytic complex of full-length Aa-RNase III with dsRNA. Here, we present the crystal structure of Aa-RNase III in complex with dsRNA, revealing a noncatalytic assembly. The major differences between the two functional forms of RNase III.dsRNA are the conformation of the protein and the orientation and location of dsRNA. The flexibility of a 7 residue linker between the endoND and dsRBD enables the transition between these two forms.
