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TitleCrystal Structures Reveal an Induced-fit Binding of a Substrate-like Aza-peptide Epoxide to SARS Coronavirus Main Peptidase.
Journal, issue, pagesJ. Mol. Biol., Vol. 366, Page 916-932, Year 2007
Publish dateApr 27, 2006 (structure data deposition date)
AuthorsLee, T.W. / Cherney, M.M. / Liu, J. / James, K.E. / Powers, J.C. / Eltis, L.D. / James, M.N.G.
External linksJ. Mol. Biol. / PubMed:17196984
MethodsX-ray diffraction
Resolution1.82 - 2 Å
Structure data

PDB-2gt7:
Crystal structure of SARS coronavirus main peptidase at pH 6.0 in the space group P21
Method: X-RAY DIFFRACTION / Resolution: 1.82 Å

PDB-2gt8:
Crystal structure of SARS coronavirus main peptidase (with an additional Ala at the N-terminus of each protomer) in the space group P43212
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2gtb:
Crystal structure of SARS coronavirus main peptidase (with an additional Ala at the N-terminus of each protomer) inhibited by an aza-peptide epoxide in the space group P43212
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-AZP:
(5S,8S,14R)-ETHYL 11-(3-AMINO-3-OXOPROPYL)-8-BENZYL-14-HYDROXY-5-ISOBUTYL-3,6,9,12-TETRAOXO-1-PHENYL-2-OXA-4,7,10,11-TETRAAZAPENTADECAN-15-OATE

ChemComp-ACY:
ACETIC ACID

Source
  • sars coronavirus
KeywordsHYDROLASE / cysteine peptidase / 3C-like / N-finger / chymotrypsin-like fold / long loop / alpha-helical domain / dimer / catalytic dyad / specificity pockets

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