5UTV

SARS-unique fold in the Rousettus Bat Coronavirus HKU9

5UTV の概要

• エントリーDOI: 10.2210/pdb5utv/pdb
• NMR情報: BMRB: 30247
• 分子名称: Papain-like proteinase (1 entity in total)
• 機能のキーワード: coronavirus, nonstructural protein 3, hku9, sars-unique domain, viral protein
• 由来する生物種: Rousettus bat coronavirus HKU9 (BtCoV)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8736.02

構造登録者

Hammond, R.G.,Tan, X.,Johnson, M.A. (登録日: 2017-02-15, 公開日: 2017-06-21, 最終更新日: 2024-05-15)

主引用文献

Hammond, R.G.,Tan, X.,Johnson, M.A.
SARS-unique fold in the Rousettus bat coronavirus HKU9.
Protein Sci., 26:1726-1737, 2017

PubMed Abstract: The coronavirus nonstructural protein 3 (nsp3) is a multifunctional protein that comprises multiple structural domains. This protein assists viral polyprotein cleavage, host immune interference, and may play other roles in genome replication or transcription. Here, we report the solution NMR structure of a protein from the "SARS-unique region" of the bat coronavirus HKU9. The protein contains a frataxin fold or double-wing motif, which is an α + β fold that is associated with protein/protein interactions, DNA binding, and metal ion binding. High structural similarity to the human severe acute respiratory syndrome (SARS) coronavirus nsp3 is present. A possible functional site that is conserved among some betacoronaviruses has been identified using bioinformatics and biochemical analyses. This structure provides strong experimental support for the recent proposal advanced by us and others that the "SARS-unique" region is not unique to the human SARS virus, but is conserved among several different phylogenetic groups of coronaviruses and provides essential functions.

PubMed: 28580734
DOI: 10.1002/pro.3208

実験手法

SOLUTION NMR