2ez6
From Proteopedia
Crystal structure of Aquifex aeolicus RNase III (D44N) complexed with product of double-stranded RNA processing
Overview
Members of the ribonuclease III (RNase III) family are double-stranded RNA (dsRNA) specific endoribonucleases characterized by a signature motif in their active centers and a two-base 3' overhang in their products. While Dicer, which produces small interfering RNAs, is currently the focus of intense interest, the structurally simpler bacterial RNase III serves as a paradigm for the entire family. Here, we present the crystal structure of an RNase III-product complex, the first catalytic complex observed for the family. A 7 residue linker within the protein facilitates induced fit in protein-RNA recognition. A pattern of protein-RNA interactions, defined by four RNA binding motifs in RNase III and three protein-interacting boxes in dsRNA, is responsible for substrate specificity, while conserved amino acid residues and divalent cations are responsible for scissile-bond cleavage. The structure reveals a wealth of information about the mechanism of RNA hydrolysis that can be extrapolated to other RNase III family members.
About this Structure
2EZ6 is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
Reference
Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III., Gan J, Tropea JE, Austin BP, Court DL, Waugh DS, Ji X, Cell. 2006 Jan 27;124(2):355-66. PMID:16439209 Page seeded by OCA on Sun May 4 03:16:31 2008
