8old | pdb_00008old

Crystal structure of Archaeoglobus fulgidus AfAgo-N protein representing N-L1-L2 domains

spinqualitylabelsall models 8old, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8old is a 2 chain structure with sequence from Archaeoglobus fulgidus DSM 8774. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: CAC, CL, MPD, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A075WKW4_ARCFL Publication Abstract from PubMed Argonaute (Ago) proteins are present in all three domains of life (bacteria, archaea and eukaryotes). They use small (15-30 nucleotides) oligonucleotide guides to bind complementary nucleic acid targets and are responsible for gene expression regulation, mobile genome element silencing, and defence against viruses or plasmids. According to their domain organization, Agos are divided into long and short Agos. Long Agos found in prokaryotes (long-A and long-B pAgos) and eukaryotes (eAgos) comprise four major functional domains (N, PAZ, MID and PIWI) and two structural linker domains L1 and L2. The majority ( approximately 60%) of pAgos are short pAgos, containing only the MID and inactive PIWI domains. Here we focus on the prokaryotic Argonaute AfAgo from Archaeoglobus fulgidus DSM4304. Although phylogenetically classified as a long-B pAgo, AfAgo contains only MID and catalytically inactive PIWI domains, akin to short pAgos. We show that AfAgo forms a heterodimeric complex with a protein encoded upstream in the same operon, which is a structural equivalent of the N-L1-L2 domains of long pAgos. This complex, structurally equivalent to a long PAZ-less pAgo, outperforms standalone AfAgo in guide RNA-mediated target DNA binding. Our findings provide a missing piece to one of the first and the most studied pAgos. The missing part: the Archaeoglobus fulgidus Argonaute forms a functional heterodimer with an N-L1-L2 domain protein.,Manakova E, Golovinas E, Poceviciute R, Sasnauskas G, Silanskas A, Rutkauskas D, Jankunec M, Zagorskaite E, Jurgelaitis E, Grybauskas A, Venclovas C, Zaremba M Nucleic Acids Res. 2024 Jan 9:gkad1241. doi: 10.1093/nar/gkad1241. PMID:38197228 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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