SNAP annotations: PDB entry 1rc7

PDB-id

1rc7; DSSR-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.