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Severe acute respiratory syndrome coronavirus papain-like protease: Structure of a viral deubiquitinating enzyme

Academic Article
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Overview

authors

  • Ratia, K.
  • Saikatendu, K. S.
  • Santarsiero, B. D.
  • Barretto, N.
  • Baker, S. C.
  • Stevens, Raymond
  • Mesecar, A. D.

publication date

  • April 2006

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • 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.

subject areas

  • Binding Sites
  • Crystallography, X-Ray
  • Cysteine Endopeptidases
  • Models, Molecular
  • Papain
  • Peptide Hydrolases
  • Protein Structure, Secondary
  • SARS Virus
  • Ubiquitin
  • Viral Proteins
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Research

keywords

  • membrane-associated protease
  • ubiquitin-like domain
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Identity

PubMed Central ID

  • PMC1458639

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0510851103

PubMed ID

  • 16581910
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Additional Document Info

start page

  • 5717

end page

  • 5722

volume

  • 103

issue

  • 15

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