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3ZC0

Structure of AfC3PO - duplex RNA complex

Summary for 3ZC0
Entry DOI10.2210/pdb3zc0/pdb
Related3ZC1
DescriptorAFTRAX, 5'-R(*UP*UP*CP*GP*AP*CP*GP*CP*GP*UP*CP*GP*AP*AP*UP*U)-3', MAGNESIUM ION, ... (5 entities in total)
Functional Keywordshydrolase-rna complex, translin, trax, rna interference, rnai, rna silencing, sirna, passenger strand, risc, hydrolase/rna
Biological sourceARCHAEOGLOBUS FULGIDUS
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Total number of polymer chains15
Total formula weight289251.34
Authors
Parizotto, E.A.,Lowe, E.D.,Parker, J.S. (deposition date: 2012-11-14, release date: 2013-01-23, Last modification date: 2023-12-20)
Primary citationParizotto, E.A.,Lowe, E.D.,Parker, J.S.
Structural Basis for Duplex RNA Recognition and Cleavage by Archaeoglobus Fulgidus C3Po.
Nat.Struct.Mol.Biol., 20:380-, 2013
Cited by
PubMed Abstract: Oligomeric complexes of Trax and Translin proteins, known as C3POs, participate in several eukaryotic nucleic acid metabolism pathways, including RNA interference and tRNA processing. In RNA interference in humans and Drosophila, C3PO activates the RNA-induced silencing complex (RISC) by removing the passenger strand of the small interfering RNA precursor duplex, using nuclease activity present in Trax. How C3POs engage with nucleic acid substrates is unknown. Here we identify a single protein from Archaeoglobus fulgidus that assembles into an octamer highly similar to human C3PO. The structure in complex with duplex RNA reveals that the octamer entirely encapsulates a single 13-base-pair RNA duplex inside a large inner cavity. Trax-like-subunit catalytic sites target opposite strands of the duplex for cleavage separated by 7 base pairs. The structure provides insight into the mechanism of RNA recognition and cleavage by an archaeal C3PO-like complex.
PubMed: 23353787
DOI: 10.1038/NSMB.2487
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.982 Å)
Structure validation

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