Crystal Structure of Middle East Respiratory Syndrome Coronavirus Helicase

Overview

Journal PLoS Pathog

Specialty Microbiology

Date 2017 Jun 27

PMID 28651017

Citations 62

Authors

Wei Hao

Justyna Aleksandra Wojdyla

Rong Zhao

Ruiyun Han

Rajat Das

Ivan Zlatev

Muthiah Manoharan

Meitian Wang

Sheng Cui

Affiliations

Soon will be listed here.

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.

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