5JRC

Crystal structure of NeC3PO in complex with ssRNA.

5JRC の概要

• エントリーDOI: 10.2210/pdb5jrc/pdb
• 関連するPDBエントリー: 5JR9 5JRE
• 分子名称: NEQ131, ssRNA, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: c3po, complex, dna binding protein
• 由来する生物種: Nanoarchaeum equitans (strain Kin4-M); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 105627.01

構造登録者

Zhang, J.,Gan, J. (登録日: 2016-05-06, 公開日: 2016-09-28, 最終更新日: 2024-03-20)

主引用文献

Zhang, J.,Liu, H.,Yao, Q.,Yu, X.,Chen, Y.,Cui, R.,Wu, B.,Zheng, L.,Zuo, J.,Huang, Z.,Ma, J.,Gan, J.
Structural basis for single-stranded RNA recognition and cleavage by C3PO
Nucleic Acids Res., 44:9494-9504, 2016

PubMed Abstract: Translin and translin-associated factor-x are highly conserved in eukaroytes; they can form heteromeric complexes (known as C3POs) and participate in various nucleic acid metabolism pathways. In humans and Drosophila, C3POs cleave the fragmented siRNA passenger strands and facilitate the activation of RNA-induced silencing complex, the effector complex of RNA interference (RNAi). Here, we report three crystal structures of Nanoarchaeum equitans (Ne) C3PO. The apo-NeC3PO structure adopts an open form and unravels a potential substrates entryway for the first time. The NeC3PO:ssRNA and NeC3PO:ssDNA complexes fold like closed football with the substrates captured at the inner cavities. The NeC3PO:ssRNA structure represents the only catalytic form C3PO complex available to date; with mutagenesis and in vitro cleavage assays, the structure provides critical insights into the substrate binding and the two-cation-assisted catalytic mechanisms that are shared by eukaryotic C3POs. The work presented here further advances our understanding on the RNAi pathway.

PubMed: 27596600
DOI: 10.1093/nar/gkw776

実験手法

X-RAY DIFFRACTION (1.9 Å)