Preparation and Crystallization of Picornain 3C of Rhinovirus A28-Reference-Cited by-同舟云学术

Preparation and Crystallization of Picornain 3C of Rhinovirus A28

Published:2023-11-01 Issue:6 Volume:68 Page:926-933
ISSN:0023-4761
Container-title:Кристаллография
language:
Short-container-title:Kristallografiâ

Author:

Tishin A. E.¹,Gladysheva A. V.²^ORCID,Pyatavina L. A.¹³,Olkin S. E.¹,Gladysheva A. A.²⁴^ORCID,Imatdionov I. R.¹,Vlaskina A. V.⁵,Nikolaeva A. Yu.⁵,Samygina V. R.⁶⁷,Agafonov A. P.¹

Affiliation:

1. State Research Center of Virology and Biotechnology “Vector,” Rospotrebnadzor, 630559, Koltsovo, Novosibirsk oblast, Russia

2. State Scientific Center of Virology and Biotechnology «Vector»

3. Novosibirsk National Research State University, 630090, Novosibirsk, Russia

4. Novosibirsk National Research State University

5. National Research Centre “Kurchatov Institute”, 123098, Moscow, Russia

6. National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia

7. Shubnikov Institute of Crystallography, Federal Scientific Research Centre “Crystallography and Photonics,” Russian Academy of Sciences, 119333, Moscow, Russia

Abstract

Human rhinovirus picornain 3C is a high-value commercial cysteine protease, which is widely used to remove affinity tags and fusion proteins during the purification of the target proteins. A variant of rhinovirus A28 picornain 3C produced in this study is not annotated in the NCBI databases, shares 79% sequence identity in the PDB, and was not previously used in the protein engineering. A protocol was developed for the isolation and purification of the protein to use it in structural studies. The initial crystallization conditions were found. The determination and analysis of the structure of rhinovirus A28 picornain 3C will provide new possibilities for performing basic research on the evolution of proteolytic enzymes and for the design of the optimal variant of this protease.

Publisher

The Russian Academy of Sciences

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