1U04
Crystal structure of full length Argonaute from Pyrococcus furiosus
Summary for 1U04
Entry DOI | 10.2210/pdb1u04/pdb |
Descriptor | hypothetical protein PF0537 (2 entities in total) |
Functional Keywords | rnai, silencing, argonaute, piwi, paz, risc, slicer, rnase h, hydrolase-gene regulation complex, hydrolase/gene regulation |
Biological source | Pyrococcus furiosus |
Total number of polymer chains | 1 |
Total formula weight | 91441.30 |
Authors | Song, J.J.,Smith, S.K.,Hannon, G.J.,Joshua-Tor, L. (deposition date: 2004-07-12, release date: 2004-08-17, Last modification date: 2024-10-30) |
Primary citation | Song, J.J.,Smith, S.K.,Hannon, G.J.,Joshua-Tor, L. Crystal Structure of Argonaute and Its Implications for RISC Slicer Activity Science, 305:1434-1437, 2004 Cited by PubMed Abstract: Argonaute proteins and small interfering RNAs (siRNAs) are the known signature components of the RNA interference effector complex RNA-induced silencing complex (RISC). However, the identity of "Slicer," the enzyme that cleaves the messenger RNA (mRNA) as directed by the siRNA, has not been resolved. Here, we report the crystal structure of the Argonaute protein from Pyrococcus furiosus at 2.25 angstrom resolution. The structure reveals a crescent-shaped base made up of the amino-terminal, middle, and PIWI domains. The Piwi Argonaute Zwille (PAZ) domain is held above the base by a "stalk"-like region. The PIWI domain (named for the protein piwi) is similar to ribonuclease H, with a conserved active site aspartate-aspartate-glutamate motif, strongly implicating Argonaute as "Slicer." The architecture of the molecule and the placement of the PAZ and PIWI domains define a groove for substrate binding and suggest a mechanism for siRNA-guided mRNA cleavage. PubMed: 15284453DOI: 10.1126 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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