1rc5
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CRYSTAL STRUCTURE OF MG(II)-COMPLEX OF RNASE III ENDONUCLEASE DOMAIN FROM AQUIFEX AEOLICUS AT 2.30 ANGSTROM RESOLUTION
OverviewOverview
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.
About this StructureAbout this Structure
1RC5 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.
ReferenceReference
Noncatalytic assembly of ribonuclease III with double-stranded RNA., Blaszczyk J, Gan J, Tropea JE, Court DL, Waugh DS, Ji X, Structure. 2004 Mar;12(3):457-66. PMID:15016361
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