2ez6
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(New page: 200px<br /><applet load="2ez6" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ez6, resolution 2.05Å" /> '''Crystal structure of...)
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Revision as of 08:07, 21 November 2007
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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 with MG as ligand. Active as Ribonuclease III, with EC number 3.1.26.3 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
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