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| - | [[Image:1i4s.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1i4s| PDB=1i4s | SCENE= }} | | {{STRUCTURE_1i4s| PDB=1i4s | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF RNASE III ENDONUCLEASE DOMAIN FROM AQUIFEX AEOLICUS AT 2.15 ANGSTROM RESOLUTION'''
| + | ===CRYSTAL STRUCTURE OF RNASE III ENDONUCLEASE DOMAIN FROM AQUIFEX AEOLICUS AT 2.15 ANGSTROM RESOLUTION=== |
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| - | ==Overview==
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| - | 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 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. RESULTS: We present the crystal structures of the Aa-RNase III endonuclease domain in its ligand-free form and in complex with Mn(2+). The structures reveal a novel protein fold and suggest a mechanism for dsRNA cleavage. On the basis of structural, genetic, and biological data, we have constructed a hypothetical model of Aa-RNase III in complex with dsRNA and Mg(2+) ion, which provides the first glimpse of RNase III in action. CONCLUSIONS: The functional Aa-RNase III dimer is formed via mainly hydrophobic interactions, including a "ball-and-socket" junction that ensures accurate alignment of the two monomers. The fold of the polypeptide chain and its dimerization create a valley with two compound active centers at each end of the valley. The valley can accommodate a dsRNA substrate. Mn(2+) binding has significant impact on crystal packing, intermolecular interactions, thermal stability, and the formation of two RNA-cutting sites within each compound active center.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11738048}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11738048 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11738048}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Ribonuclease]] | | [[Category: Ribonuclease]] |
| | [[Category: Rnase iii]] | | [[Category: Rnase iii]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:34:23 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:25:08 2008'' |
Revision as of 07:25, 1 July 2008
Template:STRUCTURE 1i4s
CRYSTAL STRUCTURE OF RNASE III ENDONUCLEASE DOMAIN FROM AQUIFEX AEOLICUS AT 2.15 ANGSTROM RESOLUTION
Template:ABSTRACT PUBMED 11738048
About this Structure
1I4S is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
Reference
Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage., Blaszczyk J, Tropea JE, Bubunenko M, Routzahn KM, Waugh DS, Court DL, Ji X, Structure. 2001 Dec;9(12):1225-36. PMID:11738048
Page seeded by OCA on Tue Jul 1 10:25:08 2008
