6OAW

Crystal structure of a CRISPR Cas-related protein

6OAW の概要

• エントリーDOI: 10.2210/pdb6oaw/pdb
• 分子名称: WYL1, UNKNOWN LIGAND (3 entities in total)
• 機能のキーワード: wyl domain, structural genomics, structural genomics consortium, sgc, immune system
• 由来する生物種: Ruminococcus sp.
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91988.43

構造登録者

Zhang, H.,Dong, C.,Li, L.,Tempel, W.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (登録日: 2019-03-18, 公開日: 2019-04-10, 最終更新日: 2025-10-22)

主引用文献

Zhang, H.,Dong, C.,Li, L.,Wasney, G.A.,Min, J.
Structural insights into the modulatory role of the accessory protein WYL1 in the Type VI-D CRISPR-Cas system.
Nucleic Acids Res., 47:5420-5428, 2019

PubMed Abstract: The Type VI-D CRISPR-Cas system employs an RNA-guided RNase Cas13d with minimal targeting constraints to combat viral infections. This CRISPR system contains RspWYL1 as a unique accessory protein that plays a key role in boosting its effector function on target RNAs, but the mechanism behind this RspWYL1-mediated stimulation remains completely unexplored. Through structural and biophysical approaches, we reveal that the full-length RspWYL1 possesses a novel three-domain architecture and preferentially binds ssRNA with high affinity. Specifically, the N-terminus of RspWYL1 harbors a ribbon-helix-helix motif reminiscent of transcriptional regulators; the central WYL domain of RspWYL1 displays a Sm-like β-barrel fold; and the C-terminal domain of RspWYL1 primarily contributes to the dimerization of RspWYL1 and may regulate the RspWYL1 function via a large conformational change. Collectively, this study provides a first glimpse into the complex mechanism behind the RspWYL1-dictated boosting of target ssRNA cleavage in the Type VI-D CRISPR-Cas system.

PubMed: 30976796
DOI: 10.1093/nar/gkz269

実験手法

X-RAY DIFFRACTION (2.2 Å)