5WWP

Crystal structure of Middle East respiratory syndrome coronavirus helicase (MERS-CoV nsp13)

5WWP の概要

• エントリーDOI: 10.2210/pdb5wwp/pdb
• 分子名称: ORF1ab, ZINC ION, SULFATE ION (3 entities in total)
• 機能のキーワード: middle east respiratory syndrome coronavirus, nidovirales, coronavirus, mers, nsp13, helicase, sf1 superfamily, atp hydrolysis, atpase, rna 5'-triphosphatase, unwinding, upf1 helicase, arterivirus nsp10, zinc binding domain, ch domain, 1b beta-barrel domain, viral rna synthesis, reca-like domain, cov replication and transcription, hydrolase
• 由来する生物種: Human betacoronavirus 2c EMC/2012
• 細胞内の位置: Host cytoplasm, host perinuclear region . Host membrane ; Multi-pass membrane protein : K0BWD0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 133548.54

構造登録者

Hao, W.,Wojdyla, J.A.,Zhao, R.,Han, R.,Das, R.,Zlatev, I.,Manoharan, M.,Wang, M.,Cui, S. (登録日: 2017-01-03, 公開日: 2017-07-05, 最終更新日: 2024-10-30)

主引用文献

Hao, W.,Wojdyla, J.A.,Zhao, R.,Han, R.,Das, R.,Zlatev, I.,Manoharan, M.,Wang, M.,Cui, S.
Crystal structure of Middle East respiratory syndrome coronavirus helicase
PLoS Pathog., 13:e1006474-e1006474, 2017

PubMed Abstract: Middle East respiratory syndrome coronavirus (MERS-CoV) remains a threat to public health worldwide; however, effective vaccine or drug against CoVs remains unavailable. CoV helicase is one of the three evolutionary most conserved proteins in nidoviruses, thus making it an important target for drug development. We report here the first structure of full-length coronavirus helicase, MERS-CoV nsp13. MERS-CoV helicase has multiple domains, including an N-terminal Cys/His rich domain (CH) with three zinc atoms, a beta-barrel domain and a C-terminal SF1 helicase core with two RecA-like subdomains. Our structural analyses show that while the domain organization of nsp13 is conserved throughout nidoviruses, the individual domains of nsp13 are closely related to the equivalent eukaryotic domains of Upf1 helicases. The most distinctive feature differentiating CoV helicases from eukaryotic Upf1 helicases is the interaction between CH domain and helicase core.

PubMed: 28651017
DOI: 10.1371/journal.ppat.1006474

実験手法

X-RAY DIFFRACTION (3 Å)