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TitleCrystal Structure of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Papain-like Protease Bound to Ubiquitin Facilitates Targeted Disruption of Deubiquitinating Activity to Demonstrate Its Role in Innate Immune Suppression.
Journal, issue, pagesJ. Biol. Chem., Vol. 289, Page 34667-34682, Year 2014
Publish dateSep 24, 2014 (structure data deposition date)
AuthorsBailey-Elkin, B.A. / Knaap, R.C. / Johnson, G.G. / Dalebout, T.J. / Ninaber, D.K. / van Kasteren, P.B. / Bredenbeek, P.J. / Snijder, E.J. / Kikkert, M. / Mark, B.L.
External linksJ. Biol. Chem. / PubMed:25320088
MethodsX-ray diffraction
Resolution2.15 - 2.8 Å
Structure data

PDB-4rez:
Crystal structure of the Middle-East respiratory syndrome coronavirus papain-like protease
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-4rf0:
Crystal structure of the Middle-East respiratory syndrome coronavirus papain-like protease in complex with ubiquitin (space group P6522)
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-4rf1:
Crystal structure of the Middle-East respiratory syndrome coronavirus papain-like protease in complex with ubiquitin (space group P63)
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-PGO:
S-1,2-PROPANEDIOL

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-3CN:
3-AMINOPROPANE

Source
  • human betacoronavirus 2c jordan-n3/2012
  • homo sapiens (human)
KeywordsVIRAL PROTEIN / zinc ribbon / deubiquitinase / papain-like protease / PROTEIN BINDING

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