1rc5
From Proteopedia
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| , resolution 2.30Å | |||||||
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| Ligands: | |||||||
| Gene: | RNC, AQ_946 (Aquifex aeolicus) | ||||||
| Activity: | Ribonuclease III, with EC number 3.1.26.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF MG(II)-COMPLEX OF RNASE III ENDONUCLEASE DOMAIN FROM AQUIFEX AEOLICUS AT 2.30 ANGSTROM RESOLUTION
Overview
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 Structure
1RC5 is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 13:49:34 2008
