2ez6

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(New page: 200px<br /><applet load="2ez6" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ez6, resolution 2.05&Aring;" /> '''Crystal structure of...)
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[[Image:2ez6.gif|left|200px]]<br /><applet load="2ez6" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ez6.gif|left|200px]]<br /><applet load="2ez6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ez6, resolution 2.05&Aring;" />
caption="2ez6, resolution 2.05&Aring;" />
'''Crystal structure of Aquifex aeolicus RNase III (D44N) complexed with product of double-stranded RNA processing'''<br />
'''Crystal structure of Aquifex aeolicus RNase III (D44N) complexed with product of double-stranded RNA processing'''<br />
==Overview==
==Overview==
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Members of the ribonuclease III (RNase III) family are double-stranded RNA, (dsRNA) specific endoribonucleases characterized by a signature motif in, their active centers and a two-base 3' overhang in their products. While, Dicer, which produces small interfering RNAs, is currently the focus of, intense interest, the structurally simpler bacterial RNase III serves as a, paradigm for the entire family. Here, we present the crystal structure of, an RNase III-product complex, the first catalytic complex observed for the, family. A 7 residue linker within the protein facilitates induced fit in, protein-RNA recognition. A pattern of protein-RNA interactions, defined by, four RNA binding motifs in RNase III and three protein-interacting boxes, in dsRNA, is responsible for substrate specificity, while conserved amino, acid residues and divalent cations are responsible for scissile-bond, cleavage. The structure reveals a wealth of information about the, mechanism of RNA hydrolysis that can be extrapolated to other RNase III, family members.
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Members of the ribonuclease III (RNase III) family are double-stranded RNA (dsRNA) specific endoribonucleases characterized by a signature motif in their active centers and a two-base 3' overhang in their products. While Dicer, which produces small interfering RNAs, is currently the focus of intense interest, the structurally simpler bacterial RNase III serves as a paradigm for the entire family. Here, we present the crystal structure of an RNase III-product complex, the first catalytic complex observed for the family. A 7 residue linker within the protein facilitates induced fit in protein-RNA recognition. A pattern of protein-RNA interactions, defined by four RNA binding motifs in RNase III and three protein-interacting boxes in dsRNA, is responsible for substrate specificity, while conserved amino acid residues and divalent cations are responsible for scissile-bond cleavage. The structure reveals a wealth of information about the mechanism of RNA hydrolysis that can be extrapolated to other RNase III family members.
==About this Structure==
==About this Structure==
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2EZ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_III Ribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.3 3.1.26.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2EZ6 OCA].
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2EZ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_III Ribonuclease III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.3 3.1.26.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZ6 OCA].
==Reference==
==Reference==
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[[Category: Ribonuclease III]]
[[Category: Ribonuclease III]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Austin, B.P.]]
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[[Category: Austin, B P.]]
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[[Category: Court, D.L.]]
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[[Category: Court, D L.]]
[[Category: Gan, J.]]
[[Category: Gan, J.]]
[[Category: Ji, X.]]
[[Category: Ji, X.]]
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[[Category: Tropea, J.E.]]
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[[Category: Tropea, J E.]]
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[[Category: Waugh, D.S.]]
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[[Category: Waugh, D S.]]
[[Category: MG]]
[[Category: MG]]
[[Category: dsrna]]
[[Category: dsrna]]
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[[Category: rna processing]]
[[Category: rna processing]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:14:39 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:16:07 2008''

Revision as of 15:16, 21 February 2008


2ez6, resolution 2.05Å

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Crystal structure of Aquifex aeolicus RNase III (D44N) complexed with product of double-stranded RNA processing

Overview

Members of the ribonuclease III (RNase III) family are double-stranded RNA (dsRNA) specific endoribonucleases characterized by a signature motif in their active centers and a two-base 3' overhang in their products. While Dicer, which produces small interfering RNAs, is currently the focus of intense interest, the structurally simpler bacterial RNase III serves as a paradigm for the entire family. Here, we present the crystal structure of an RNase III-product complex, the first catalytic complex observed for the family. A 7 residue linker within the protein facilitates induced fit in protein-RNA recognition. A pattern of protein-RNA interactions, defined by four RNA binding motifs in RNase III and three protein-interacting boxes in dsRNA, is responsible for substrate specificity, while conserved amino acid residues and divalent cations are responsible for scissile-bond cleavage. The structure reveals a wealth of information about the mechanism of RNA hydrolysis that can be extrapolated to other RNase III family members.

About this Structure

2EZ6 is a Single protein structure of sequence from Aquifex aeolicus with as ligand. Active as Ribonuclease III, with EC number 3.1.26.3 Full crystallographic information is available from OCA.

Reference

Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III., Gan J, Tropea JE, Austin BP, Court DL, Waugh DS, Ji X, Cell. 2006 Jan 27;124(2):355-66. PMID:16439209

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