2fe8

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spinqualitylabelsall models 2fe8, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

SARS coronavirus papain-like protease: structure of a viral deubiquitinating enzyme

Overview

Replication of severe acute respiratory syndrome (SARS) coronavirus, (SARS-CoV) requires proteolytic processing of the replicase polyprotein by, two viral cysteine proteases, a chymotrypsin-like protease (3CLpro) and a, papain-like protease (PLpro). These proteases are important targets for, development of antiviral drugs that would inhibit viral replication and, reduce mortality associated with outbreaks of SARS-CoV. In this work, we, describe the 1.85-A crystal structure of the catalytic core of SARS-CoV, PLpro and show that the overall architecture adopts a fold closely, resembling that of known deubiquitinating enzymes. Key features, however, distinguish PLpro from characterized deubiquitinating enzymes, including, an intact zinc-binding motif, an unobstructed catalytically competent, active site, and the presence of an intriguing, ubiquitin-like N-terminal, domain. To gain insight into the active-site recognition of the C-terminal, tail of ubiquitin and the related LXGG motif, we propose a model of PLpro, in complex with ubiquitin-aldehyde that reveals well defined sites within, the catalytic cleft that help to account for strict substrate-recognition, motifs.

About this Structure

2FE8 is a Single protein structure of sequence from Sars coronavirus with ZN, BR and SO4 as ligands. Full crystallographic information is available from OCA.

Reference

Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme., Ratia K, Saikatendu KS, Santarsiero BD, Barretto N, Baker SC, Stevens RC, Mesecar AD, Proc Natl Acad Sci U S A. 2006 Apr 11;103(15):5717-22. Epub 2006 Mar 31. PMID:16581910

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