2EZ6

Crystal structure of Aquifex aeolicus RNase III (D44N) complexed with product of double-stranded RNA processing

Summary for 2EZ6

• Entry DOI: 10.2210/pdb2ez6/pdb
• Related: 1JFZ 1O0W 1RC5 1RC7 1YYK 1YYO 1YYW 1YZ9
• Descriptor: 28-MER, Ribonuclease III, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: ribonuclease iii, dsrna, rna processing, rna interference, hydrolase-rna complex, hydrolase/rna
• Biological source: Aquifex aeolicus
• Cellular location: Cytoplasm (By similarity): O67082
• Total number of polymer chains: 4
• Total formula weight: 70302.13

Authors

Gan, J.,Tropea, J.E.,Austin, B.P.,Court, D.L.,Waugh, D.S.,Ji, X. (deposition date: 2005-11-10, release date: 2006-02-07, Last modification date: 2023-08-30)

Primary citation

Gan, J.,Tropea, J.E.,Austin, B.P.,Court, D.L.,Waugh, D.S.,Ji, X.
Structural Insight into the Mechanism of Double-Stranded RNA Processing by Ribonuclease III.
Cell(Cambridge,Mass.), 124:355-366, 2006

PubMed Abstract: 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.

PubMed: 16439209
DOI: 10.1016/j.cell.2005.11.034

Experimental method

X-RAY DIFFRACTION (2.05 Å)