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2BGG

The structure of a Piwi protein from Archaeoglobus fulgidus complexed with a 16nt siRNA duplex.

Summary for 2BGG
Entry DOI10.2210/pdb2bgg/pdb
Related1W9H
DescriptorPROTEIN AF1318, 5'-R(*UP*UP*CP*GP*AP*CP*GP*CP)-3', 5'-R(*GP*UP*CP*GP*AP*AP*UP*UP)-3', ... (5 entities in total)
Functional Keywordsrna-binding protein-rna complex, rna-binding argonaute, piwi domain, rnai, risc, protein-rna complex, rna-binding protein/rna
Biological sourceARCHAEOGLOBUS FULGIDUS
Total number of polymer chains6
Total formula weight108774.91
Authors
Parker, J.S.,Roe, S.M.,Barford, D. (deposition date: 2004-12-22, release date: 2005-03-31, Last modification date: 2023-12-13)
Primary citationParker, J.S.,Roe, S.M.,Barford, D.
Structural Insights Into Mrna Recognition from a Piwi Domain-Sirna Guide Complex
Nature, 434:663-, 2005
Cited by
PubMed Abstract: RNA interference and related RNA silencing phenomena use short antisense guide RNA molecules to repress the expression of target genes. Argonaute proteins, containing amino-terminal PAZ (for PIWI/Argonaute/Zwille) domains and carboxy-terminal PIWI domains, are core components of these mechanisms. Here we show the crystal structure of a Piwi protein from Archaeoglobus fulgidus (AfPiwi) in complex with a small interfering RNA (siRNA)-like duplex, which mimics the 5' end of a guide RNA strand bound to an overhanging target messenger RNA. The structure contains a highly conserved metal-binding site that anchors the 5' nucleotide of the guide RNA. The first base pair of the duplex is unwound, separating the 5' nucleotide of the guide from the complementary nucleotide on the target strand, which exits with the 3' overhang through a short channel. The remaining base-paired nucleotides assume an A-form helix, accommodated within a channel in the PIWI domain, which can be extended to place the scissile phosphate of the target strand adjacent to the putative slicer catalytic site. This study provides insights into mechanisms of target mRNA recognition and cleavage by an Argonaute-siRNA guide complex.
PubMed: 15800628
DOI: 10.1038/NATURE03462
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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数据于2024-11-06公开中

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