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Article Name
Structural insights into RISC assembly facilitated by dsRNA-binding domains of human RNA helicase A (DHX9).
Protein Name
Name: 2EZ6
The protein 2ez6 seems to be first discovered in the "Aquifex aeolicus" is a rod-shaped bacterium with a length of 2 to 6 micrometers and a diameter of around half a micrometer.The protein itself is a 2ez6 is a 4 chain structure with a sequence form.
Protein Function
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.
Relevance
2EZ6 - Crystal structure of Aquifex aeolicus RNase III (D44N) complexed with product of double-stranded RNA processing. It is an important part of RNA processig because the RNA copy of a protein encoding gene must be modified in several ways before it can be transported out of the nucleus and translated into protein. Meanwhile RNA
Structural Highlights
this link show this part of the protein
