1I4S

CRYSTAL STRUCTURE OF RNASE III ENDONUCLEASE DOMAIN FROM AQUIFEX AEOLICUS AT 2.15 ANGSTROM RESOLUTION

Summary for 1I4S

• Entry DOI: 10.2210/pdb1i4s/pdb
• Related: 1DI2 1STU
• Descriptor: RIBONUCLEASE III (2 entities in total)
• Functional Keywords: ribonuclease, rnase iii, double-stranded rna, catalytic domain, endonuclease domain, endonucleolytic cleavage, hydrolase
• Biological source: Aquifex aeolicus
• Cellular location: Cytoplasm : O67082
• Total number of polymer chains: 2
• Total formula weight: 34554.16

Authors

Blaszczyk, J.,Ji, X. (deposition date: 2001-02-22, release date: 2001-12-19, Last modification date: 2023-08-30)

Primary citation

Blaszczyk, J.,Tropea, J.E.,Bubunenko, M.,Routzahn, K.M.,Waugh, D.S.,Court, D.L.,Ji, X.
Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage.
Structure, 9:1225-1236, 2001

PubMed Abstract: Aquifex aeolicus Ribonuclease III (Aa-RNase III) belongs to the family of Mg(2+)-dependent endonucleases that show specificity for double-stranded RNA (dsRNA). RNase III is conserved in all known bacteria and eukaryotes and has 1-2 copies of a 9-residue consensus sequence, known as the RNase III signature motif. The bacterial RNase III proteins are the simplest, consisting of two domains: an N-terminal endonuclease domain, followed by a double-stranded RNA binding domain (dsRBD). The three-dimensional structure of the dsRBD in Escherichia coli RNase III has been elucidated; no structural information is available for the endonuclease domain of any RNase III.

PubMed: 11738048
DOI: 10.1016/S0969-2126(01)00685-2

Experimental method

X-RAY DIFFRACTION (2.15 Å)