8OLJ

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

8OLJ の概要

• エントリーDOI: 10.2210/pdb8olj/pdb
• 関連するPDBエントリー: 8OK9 8OLD
• 分子名称: Archaeoglobus fulgidus AfAgo-N protein representing N-L1-L2 domains, GLYCEROL, ISOPROPYL ALCOHOL, ... (7 entities in total)
• 機能のキーワード: protein-nucleic acid interactions, argonaute, pago, guide and target specificity, protein binding, rna binding protein
• 由来する生物種: Archaeoglobus fulgidus DSM 8774
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31876.57

構造登録者

Manakova, E.N.,Zaremba, M.,Grazulis, S. (登録日: 2023-03-30, 公開日: 2024-01-24, 最終更新日: 2024-03-27)

主引用文献

Manakova, E.,Golovinas, E.,Poceviciute, R.,Sasnauskas, G.,Silanskas, A.,Rutkauskas, D.,Jankunec, M.,Zagorskaite, E.,Jurgelaitis, E.,Grybauskas, A.,Venclovas, C.,Zaremba, M.
The missing part: the Archaeoglobus fulgidus Argonaute forms a functional heterodimer with an N-L1-L2 domain protein.
Nucleic Acids Res., 52:2530-2545, 2024

PubMed Abstract: 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 (∼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.

PubMed: 38197228
DOI: 10.1093/nar/gkad1241

実験手法

X-RAY DIFFRACTION (1.4 Å)