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1U04

Crystal structure of full length Argonaute from Pyrococcus furiosus

Summary for 1U04
Entry DOI10.2210/pdb1u04/pdb
Descriptorhypothetical protein PF0537 (2 entities in total)
Functional Keywordsrnai, silencing, argonaute, piwi, paz, risc, slicer, rnase h, hydrolase-gene regulation complex, hydrolase/gene regulation
Biological sourcePyrococcus furiosus
Total number of polymer chains1
Total formula weight91441.30
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 citationSong, 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: 15284453
DOI: 10.1126
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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