6WUI

Crystal Structure of mutant S. pombe Rai1 (E150S/E199Q/E239Q) in complex with 3'-FADP

6WUI の概要

• エントリーDOI: 10.2210/pdb6wui/pdb
• 分子名称: Decapping nuclease din1, [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (2R,3S,4S)-5-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)-2,3,4-trihydroxypentyl dihydrogen diphosphate (non-preferred name) (3 entities in total)
• 機能のキーワード: fad, 3'-fadp, rna, cap, decapping, hydrolase, rai1
• 由来する生物種: Schizosaccharomyces pombe (Fission yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43792.53

構造登録者

Doamekpor, S.K.,Tong, L. (登録日: 2020-05-04, 公開日: 2020-05-20, 最終更新日: 2023-10-18)

主引用文献

Doamekpor, S.K.,Grudzien-Nogalska, E.,Mlynarska-Cieslak, A.,Kowalska, J.,Kiledjian, M.,Tong, L.
DXO/Rai1 enzymes remove 5'-end FAD and dephospho-CoA caps on RNAs.
Nucleic Acids Res., 48:6136-6148, 2020

PubMed Abstract: In eukaryotes, the DXO/Rai1 enzymes can eliminate most of the incomplete and non-canonical NAD caps through their decapping, deNADding and pyrophosphohydrolase activities. Here, we report that these enzymes can also remove FAD and dephospho-CoA (dpCoA) non-canonical caps from RNA, and we have named these activities deFADding and deCoAping. The crystal structures of mammalian DXO with 3'-FADP or CoA and fission yeast Rai1 with 3'-FADP provide elegant insight to these activities. FAD and CoA are accommodated in the DXO/Rai1 active site by adopting folded conformations. The flavin of FAD and the pantetheine group of CoA contact the same region at the bottom of the active site tunnel, which undergoes conformational changes to accommodate the different cap moieties. We have developed FAD-capQ to detect and quantify FAD-capped RNAs and determined that FAD caps are present on short RNAs (with less than ∼200 nucleotides) in human cells and that these RNAs are stabilized in the absence of DXO.

PubMed: 32374864
DOI: 10.1093/nar/gkaa297

実験手法

X-RAY DIFFRACTION (1.9 Å)