2f8s

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(New page: 200px<br /><applet load="2f8s" size="350" color="white" frame="true" align="right" spinBox="true" caption="2f8s, resolution 3.00&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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Argonaute proteins are key components of the RNA-induced silencing complex, (RISC). They provide both architectural and catalytic functionalities, associated with small interfering RNA (siRNA) guide strand recognition and, subsequent guide strand-mediated cleavage of complementary mRNAs. We, report on the 3.0 A crystal structures of 22-mer and 26-mer siRNAs bound, to Aquifex aeolicus Argonaute (Aa-Ago), where one 2 nt 3' overhang of the, siRNA inserts into a cavity positioned on the outer surface of the, PAZ-containing lobe of the bilobal Aa-Ago architecture. The first overhang, nucleotide stacks over a tyrosine ring, while the second overhang, nucleotide, together with the intervening sugar-phosphate backbone, inserts into a preformed surface cavity. Photochemical crosslinking, studies on Aa-Ago with 5-iodoU-labeled single-stranded siRNA and siRNA, duplex provide support for this externally bound siRNA-Aa-Ago complex. The, structure and biochemical data together provide insights into a, protein-RNA recognition event potentially associated with the RISC-loading, pathway.
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Argonaute proteins are key components of the RNA-induced silencing complex (RISC). They provide both architectural and catalytic functionalities associated with small interfering RNA (siRNA) guide strand recognition and subsequent guide strand-mediated cleavage of complementary mRNAs. We report on the 3.0 A crystal structures of 22-mer and 26-mer siRNAs bound to Aquifex aeolicus Argonaute (Aa-Ago), where one 2 nt 3' overhang of the siRNA inserts into a cavity positioned on the outer surface of the PAZ-containing lobe of the bilobal Aa-Ago architecture. The first overhang nucleotide stacks over a tyrosine ring, while the second overhang nucleotide, together with the intervening sugar-phosphate backbone, inserts into a preformed surface cavity. Photochemical crosslinking studies on Aa-Ago with 5-iodoU-labeled single-stranded siRNA and siRNA duplex provide support for this externally bound siRNA-Aa-Ago complex. The structure and biochemical data together provide insights into a protein-RNA recognition event potentially associated with the RISC-loading pathway.
==About this Structure==
==About this Structure==
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[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chen, H.Y.]]
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[[Category: Chen, H Y.]]
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[[Category: Patel, D.J.]]
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[[Category: Patel, D J.]]
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[[Category: Yuan, Y.R.]]
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[[Category: Yuan, Y R.]]
[[Category: argonaute]]
[[Category: argonaute]]
[[Category: risc loading complex]]
[[Category: risc loading complex]]
[[Category: sirna]]
[[Category: sirna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:30:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:18:53 2008''

Revision as of 15:18, 21 February 2008


2f8s, resolution 3.00Å

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Crystal structure of Aa-Ago with externally-bound siRNA

Overview

Argonaute proteins are key components of the RNA-induced silencing complex (RISC). They provide both architectural and catalytic functionalities associated with small interfering RNA (siRNA) guide strand recognition and subsequent guide strand-mediated cleavage of complementary mRNAs. We report on the 3.0 A crystal structures of 22-mer and 26-mer siRNAs bound to Aquifex aeolicus Argonaute (Aa-Ago), where one 2 nt 3' overhang of the siRNA inserts into a cavity positioned on the outer surface of the PAZ-containing lobe of the bilobal Aa-Ago architecture. The first overhang nucleotide stacks over a tyrosine ring, while the second overhang nucleotide, together with the intervening sugar-phosphate backbone, inserts into a preformed surface cavity. Photochemical crosslinking studies on Aa-Ago with 5-iodoU-labeled single-stranded siRNA and siRNA duplex provide support for this externally bound siRNA-Aa-Ago complex. The structure and biochemical data together provide insights into a protein-RNA recognition event potentially associated with the RISC-loading pathway.

About this Structure

2F8S is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

Reference

A potential protein-RNA recognition event along the RISC-loading pathway from the structure of A. aeolicus Argonaute with externally bound siRNA., Yuan YR, Pei Y, Chen HY, Tuschl T, Patel DJ, Structure. 2006 Oct;14(10):1557-65. PMID:17027504

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