1ytu: Difference between revisions

Revision as of 17:02, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ytu.png

Template:STRUCTURE 1ytu

Structural basis for 5'-end-specific recognition of the guide RNA strand by the A. fulgidus PIWI proteinStructural basis for 5'-end-specific recognition of the guide RNA strand by the A. fulgidus PIWI protein

Template:ABSTRACT PUBMED 15800629

About this StructureAbout this Structure

1YTU is a Single protein structure of sequence from Archaeoglobus fulgidus dsm 4304. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for 5'-end-specific recognition of guide RNA by the A. fulgidus Piwi protein., Ma JB, Yuan YR, Meister G, Pei Y, Tuschl T, Patel DJ, Nature. 2005 Mar 31;434(7033):666-70. PMID:15800629

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OCA

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-'''Structural basis for 5'-end-specific recognition of the guide RNA strand by the A. fulgidus PIWI protein'''
+===Structural basis for 5'-end-specific recognition of the guide RNA strand by the A. fulgidus PIWI protein===
-==Overview==
+<!--
-RNA interference (RNAi) is a conserved sequence-specific gene regulatory mechanism mediated by the RNA-induced silencing complex (RISC), which is composed of a single-stranded guide RNA and an Argonaute protein. The PIWI domain, a highly conserved motif within Argonaute, has been shown to adopt an RNase H fold critical for the endonuclease cleavage activity of RISC. Here we report the crystal structure of Archaeoglobus fulgidus Piwi protein bound to double-stranded RNA, thereby identifying the binding pocket for guide-strand 5'-end recognition and providing insight into guide-strand-mediated messenger RNA target recognition. The phosphorylated 5' end of the guide RNA is anchored within a highly conserved basic pocket, supplemented by the carboxy-terminal carboxylate and a bound divalent cation. The first nucleotide from the 5' end of the guide RNA is unpaired and stacks over a conserved tyrosine residue, whereas successive nucleotides form a four-base-pair RNA duplex. Mutation of the corresponding amino acids that contact the 5' phosphate in human Ago2 resulted in attenuated mRNA cleavage activity. Our structure of the Piwi-RNA complex, and that determined elsewhere, provide direct support for the 5' region of the guide RNA serving as a nucleation site for pairing with target mRNA and for a fixed distance separating the RISC-mediated mRNA cleavage site from the anchored 5' end of the guide RNA.
+The line below this paragraph, {{ABSTRACT_PUBMED_15800629}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15800629 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15800629}}
 ==About this Structure==
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 [[Category: Protein-rna complex]]
 [[Category: Rna duplex]]
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