7K9P

Room temperature structure of NSP15 Endoribonuclease from SARS CoV-2 solved using SFX.

7K9P の概要

• エントリーDOI: 10.2210/pdb7k9p/pdb
• 分子名称: Uridylate-specific endoribonuclease, CITRIC ACID (3 entities in total)
• 機能のキーワード: severe acute respiratory syndrome coronavirus 2, room temperature structure, serial femtosecond crystallography, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78743.46

構造登録者

Botha, S.,Jernigan, R.,Chen, J.,Coleman, M.A.,Frank, M.,Grant, T.D.,Hansen, D.T.,Ketawala, G.,Logeswaran, D.,Martin-Garcia, J.,Nagaratnam, N.,Raj, A.L.L.X.,Shelby, M.,Yang, J.-H.,Yung, M.C.,Fromme, P. (登録日: 2020-09-29, 公開日: 2020-10-21, 最終更新日: 2023-10-25)

主引用文献

Jernigan, R.J.,Logeswaran, D.,Doppler, D.,Nagaratnam, N.,Sonker, M.,Yang, J.H.,Ketawala, G.,Martin-Garcia, J.M.,Shelby, M.L.,Grant, T.D.,Mariani, V.,Tolstikova, A.,Sheikh, M.Z.,Yung, M.C.,Coleman, M.A.,Zaare, S.,Kaschner, E.K.,Rabbani, M.T.,Nazari, R.,Zacks, M.A.,Hayes, B.,Sierra, R.G.,Hunter, M.S.,Lisova, S.,Batyuk, A.,Kupitz, C.,Boutet, S.,Hansen, D.T.,Kirian, R.A.,Schmidt, M.,Fromme, R.,Frank, M.,Ros, A.,Chen, J.J.,Botha, S.,Fromme, P.
Room-temperature structural studies of SARS-CoV-2 protein NendoU with an X-ray free-electron laser.
Structure, 2022

PubMed Abstract: NendoU from SARS-CoV-2 is responsible for the virus's ability to evade the innate immune system by cleaving the polyuridine leader sequence of antisense viral RNA. Here we report the room-temperature structure of NendoU, solved by serial femtosecond crystallography at an X-ray free-electron laser to 2.6 Å resolution. The room-temperature structure provides insight into the flexibility, dynamics, and other intrinsic properties of NendoU, with indications that the enzyme functions as an allosteric switch. Functional studies examining cleavage specificity in solution and in crystals support the uridine-purine cleavage preference, and we demonstrate that enzyme activity is fully maintained in crystal form. Optimizing the purification of NendoU and identifying suitable crystallization conditions set the benchmark for future time-resolved serial femtosecond crystallography studies. This could advance the design of antivirals with higher efficacy in treating coronaviral infections, since drugs that block allosteric conformational changes are less prone to drug resistance.

PubMed: 36630960
DOI: 10.1016/j.str.2022.12.009

実験手法

X-RAY DIFFRACTION (2.6 Å)