1R6Z

The Crystal Structure of the Argonaute2 PAZ domain (as a MBP fusion)

Summary for 1R6Z

• Entry DOI: 10.2210/pdb1r6z/pdb
• Related PRD ID: PRD_900001
• Descriptor: Chimera of Maltose-binding periplasmic protein and Argonaute 2, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, NICKEL (II) ION, ... (4 entities in total)
• Functional Keywords: deviant ob fold, rnai, gene regulation
• Biological source: Escherichia coli (, fruit fly); More
• Total number of polymer chains: 3
• Total formula weight: 170956.09

Authors

Song, J.J.,Liu, J.,Tolia, N.H.,Schneiderman, J.,Smith, S.K.,Martienssen, R.A.,Hannon, G.J.,Joshua-Tor, L. (deposition date: 2003-10-17, release date: 2004-01-13, Last modification date: 2023-08-23)

Primary citation

Song, J.J.,Liu, J.,Tolia, N.H.,Schneiderman, J.,Smith, S.K.,Martienssen, R.A.,Hannon, G.J.,Joshua-Tor, L.
The crystal structure of the Argonaute2 PAZ domain reveals an RNA binding motif in RNAi effector complexes.
Nat.Struct.Biol., 10:1026-1032, 2003

PubMed Abstract: RISC, the RNA-induced silencing complex, uses short interfering RNAs (siRNAs) or micro RNAs (miRNAs) to select its targets in a sequence-dependent manner. Key RISC components are Argonaute proteins, which contain two characteristic domains, PAZ and PIWI. PAZ is highly conserved and is found only in Argonaute proteins and Dicer. We have solved the crystal structure of the PAZ domain of Drosophila Argonaute2. The PAZ domain contains a variant of the OB fold, a module that often binds single-stranded nucleic acids. PAZ domains show low-affinity nucleic acid binding, probably interacting with the 3' ends of single-stranded regions of RNA. PAZ can bind the characteristic two-base 3' overhangs of siRNAs, indicating that although PAZ may not be a primary nucleic acid binding site in Dicer or RISC, it may contribute to the specific and productive incorporation of siRNAs and miRNAs into the RNAi pathway.

PubMed: 14625589
DOI: 10.1038/nsb1016

Experimental method

X-RAY DIFFRACTION (2.8 Å)