About: An Episulfide Cation (Thiiranium Ring) Trapped in the Active Site of HAV 3C Proteinase Inactivated by Peptide-based Ketone Inhibitors

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About: An Episulfide Cation (Thiiranium Ring) Trapped in the Active Site of HAV 3C Proteinase Inactivated by Peptide-based Ketone Inhibitors Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	An Episulfide Cation (Thiiranium Ring) Trapped in the Active Site of HAV 3C Proteinase Inactivated by Peptide-based Ketone Inhibitors
Creator	Yin, Jiang Zhang, Jianmin Huitema, Carly Cherney, Maia Eltis, Lindsay James, Michael Vederas, John Bergmann, Ernst Pettersson, Hanna
Source	Elsevier; Medline; PMC
abstract	Abstract We have solved the crystal and molecular structures of hepatitis A viral (HAV) 3C proteinase, a cysteine peptidase having a chymotrypsin-like protein fold, in complex with each of three tetrapeptidyl-based methyl ketone inhibitors to resolutions beyond 1.4 Å, the highest resolution to date for a 3C or a 3C-Like (e.g. SARS viral main proteinase) peptidase. The residues of the β-hairpin motif (residues 138–158), an extension of two β-strands of the C-terminal β-barrel of HAV 3C are critical for the interactions between the enzyme and the tetrapeptide portion of these inhibitors that are analogous to the residues at the P4 to P1 positions in the natural substrates of picornaviral 3C proteinases. Unexpectedly, the Sγ of Cys172 forms two covalent bonds with each inhibitor, yielding an unusual episulfide cation (thiiranium ring) stabilized by a nearby oxyanion. This result suggests a mechanism of inactivation of 3C peptidases by methyl ketone inhibitors that is distinct from that occurring in the structurally related serine proteinases or in the papain-like cysteine peptidases. It also provides insight into the mechanisms underlying both the inactivation of HAV 3C by these inhibitors and on the proteolysis of natural substrates by this viral cysteine peptidase.
has issue date	2006-08-25(xsd:dateTime)
bibo:doi	10.1016/j.jmb.2006.06.047
bibo:pmid	16860823
has license	els-covid
sha1sum (hex)	7e19d787dae7e61ec5a9b0c28d42ad3baf410986
schema:url	https://doi.org/10.1016/j.jmb.2006.06.047
resource representing a document's title	An Episulfide Cation (Thiiranium Ring) Trapped in the Active Site of HAV 3C Proteinase Inactivated by Peptide-based Ketone Inhibitors
has PubMed Central identifier	PMC7172884
has PubMed identifier	16860823
schema:publication	Journal of Molecular Biology
resource representing a document's body	covid:7e19d787dae7e61ec5a9b0c28d42ad3baf410986#body_text
is schema:about of	named entity 'proteolysis' named entity 'natural' named entity 'serine' named entity 'cysteine peptidases' named entity 'stabilized' named entity 'inhibitors' named entity 'structurally' named entity 'cation' named entity 'residues' named entity 'Site' named entity 'CHYMOTRYPSIN' named entity 'SARS' named entity 'MECHANISM' named entity 'HEPATITIS A' named entity 'BARREL ' named entity 'RESULT' named entity 'THESE' named entity 'DATE' named entity 'MECHANISMS' covid:arg/7e19d787dae7e61ec5a9b0c28d42ad3baf410986 named entity 'inhibitors' named entity 'resolution' named entity 'β-hairpin' named entity 'enzyme' named entity 'viral' named entity 'complex' named entity 'critical' named entity 'viral' named entity 'tetrapeptide' named entity 'inhibitors' named entity 'Ketone' named entity 'covalent bonds' named entity 'tetrapeptide' named entity 'molecular structures' named entity 'structurally related' named entity 'HAV' named entity 'protein fold' named entity '3C proteinase' named entity 'motif' named entity 'Ketone' named entity 'Episulfide' named entity 'Active Site' named entity 'complex formation' named entity 'papain' named entity 'HAV' named entity 'imidazole ring' named entity 'Glu' named entity 'fluoride' named entity 'HAV' named entity 'atom' named entity 'HAV' named entity 'moiety' named entity 'polyprotein' named entity 'chloride' named entity 'Enzyme inhibition' named entity 'cysteine' named entity 'alkylated' named entity 'side-chain' named entity 'assay' named entity 'cysteine' named entity 'carbonyl group' named entity 'Glu' named entity 'atom' named entity 'virus' named entity 'cation' named entity '3C proteinase' named entity 'proteolytic' named entity 'protein fold' named entity 'electron density' named entity 'CCP4' named entity 'England' named entity 'HAV' named entity 'serine proteinases'

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