1RC5

CRYSTAL STRUCTURE OF MG(II)-COMPLEX OF RNASE III ENDONUCLEASE DOMAIN FROM AQUIFEX AEOLICUS AT 2.30 ANGSTROM RESOLUTION

Summary for 1RC5

• Entry DOI: 10.2210/pdb1rc5/pdb
• Related: 1DI2 1I4S 1JFZ 1O0W 1RC7 1STU
• Descriptor: Ribonuclease III, MAGNESIUM ION (3 entities in total)
• Functional Keywords: ribonuclease, rnase iii, double-stranded rna, rna interference, endonuclease domain, endonucleolytic cleavage, hydrolase
• Biological source: Aquifex aeolicus
• Cellular location: Cytoplasm (By similarity): O67082
• Total number of polymer chains: 4
• Total formula weight: 72749.27

Authors

Blaszczyk, J.,Gan, J.,Ji, X. (deposition date: 2003-11-03, release date: 2004-03-30, Last modification date: 2023-08-30)

Primary citation

Blaszczyk, J.,Gan, J.,Tropea, J.E.,Court, D.L.,Waugh, D.S.,Ji, X.
Noncatalytic Assembly of Ribonuclease III with Double-Stranded RNA.
Structure, 12:457-466, 2004

PubMed Abstract: 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.

PubMed: 15016361
DOI: 10.1016/j.str.2004.02.004

Experimental method

X-RAY DIFFRACTION (2.3 Å)