1UK3

Crystal structure of SARS Coronavirus Main Proteinase (3CLpro) At pH7.6

1UK3 の概要

• エントリーDOI: 10.2210/pdb1uk3/pdb
• 関連するPDBエントリー: 1UK2 1UK4
• 分子名称: 3C-like proteinase (2 entities in total)
• 機能のキーワード: anti-parallel b-barrel, anti-parallel a-helices, hydrolase
• 由来する生物種: SARS coronavirus
• 細胞内の位置: Non-structural protein 3: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 4: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 6: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 7: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 8: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 9: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 10: Host cytoplasm, host perinuclear region (By similarity). Helicase: Host endoplasmic reticulum-Golgi intermediate compartment (Potential). Uridylate-specific endoribonuclease: Host cytoplasm, host perinuclear region (By similarity): P59641
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67753.27

構造登録者

Yang, H.,Yang, M.,Liu, Y.,Bartlam, M.,Ding, Y.,Lou, Z.,Sun, L.,Zhou, Z.,Ye, S.,Anand, K.,Pang, H.,Gao, G.F.,Hilgenfeld, R.,Rao, Z. (登録日: 2003-08-14, 公開日: 2003-11-18, 最終更新日: 2023-12-27)

主引用文献

Yang, H.,Yang, M.,Ding, Y.,Liu, Y.,Lou, Z.,Zhou, Z.,Sun, L.,Mo, L.,Ye, S.,Pang, H.,Gao, G.F.,Anand, K.,Bartlam, M.,Hilgenfeld, R.,Rao, Z.
The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor
Proc.Natl.Acad.Sci.USA, 100:13190-13195, 2003

PubMed Abstract: A newly identified severe acute respiratory syndrome coronavirus (SARS-CoV), is the etiological agent responsible for the outbreak of SARS. The SARS-CoV main protease, which is a 33.8-kDa protease (also called the 3C-like protease), plays a pivotal role in mediating viral replication and transcription functions through extensive proteolytic processing of two replicase polyproteins, pp1a (486 kDa) and pp1ab (790 kDa). Here, we report the crystal structures of the SARS-CoV main protease at different pH values and in complex with a specific inhibitor. The protease structure has a fold that can be described as an augmented serine-protease, but with a Cys-His at the active site. This series of crystal structures, which is the first, to our knowledge, of any protein from the SARS virus, reveal substantial pH-dependent conformational changes, and an unexpected mode of inhibitor binding, providing a structural basis for rational drug design.

PubMed: 14585926
DOI: 10.1073/pnas.1835675100

実験手法

X-RAY DIFFRACTION (2.4 Å)