Crystallographic and Modeling Studies of RNase III Suggest a Mechanism for Double-Stranded RNA Cleavage

Background: 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 RN...

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Veröffentlicht in:	Structure 2001-12, Vol.9 (12), p.1225-1236
Hauptverfasser:	Blaszczyk, Jaroslaw, Tropea, Joseph E., Bubunenko, Mikhail, Routzahn, Karen M., Waugh, David S., Court, Donald L., Ji, Xinhua
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites CLEAVAGE compound active center CRYSTALLOGRAPHY Crystallography, X-Ray Dimerization dsRNA endonuclease domain Endoribonucleases - chemistry Escherichia coli Proteins Ligands Manganese - metabolism Models, Molecular Molecular Sequence Data Mutation NATIONAL SYNCHROTRON LIGHT SOURCE NSLS Nucleic Acid Conformation PARTICLE ACCELERATORS Protein Binding Protein Conformation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Ribonuclease III RNA RNA interference RNA processing RNA, Double-Stranded - metabolism RNase III Sequence Homology, Amino Acid SIMULATION
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