About: Structure of a Herpesvirus-Encoded Cysteine Protease Reveals a Unique Class of Deubiquitinating Enzymes

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About: Structure of a Herpesvirus-Encoded Cysteine Protease Reveals a Unique Class of Deubiquitinating Enzymes 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	Structure of a Herpesvirus-Encoded Cysteine Protease Reveals a Unique Class of Deubiquitinating Enzymes
Creator	Frijns, Evelyne Gaudet, Rachelle Schlieker, Christian Kattenhorn, Lisa Ploegh, Hidde Weihofen, Wilhelm
Source	Elsevier; Medline; PMC
abstract	All members of the herpesviridae contain within their large tegument protein a cysteine protease module that displays deubiquitinating activity. We report the crystal structure of the cysteine protease domain of murine cytomegalovirus M48 (M48(USP)) in a complex with a ubiquitin (Ub)-based suicide substrate. M48(USP) adopts a papain-like fold, with the active-site cysteine forming a thioether linkage to the suicide substrate. The Ub core participates in an extensive hydrophobic interaction with an exposed β hairpin loop of M48(USP). This Ub binding mode contributes to Ub specificity and is distinct from that observed in other deubiquitinating enzymes. Both the arrangement of active-site residues and the architecture of the interface with Ub lead us to classify this domain as the founding member of a previously unknown class of deubiquitinating enzymes.
has issue date	2007-03-09(xsd:dateTime)
bibo:doi	10.1016/j.molcel.2007.01.033
bibo:pmid	17349955
has license	no-cc
sha1sum (hex)	225ee16d130872aa6ade326d6342def4dafe7f37
schema:url	https://doi.org/10.1016/j.molcel.2007.01.033
resource representing a document's title	Structure of a Herpesvirus-Encoded Cysteine Protease Reveals a Unique Class of Deubiquitinating Enzymes
has PubMed Central identifier	PMC7110467
has PubMed identifier	17349955
schema:publication	Mol Cell
resource representing a document's body	covid:225ee16d130872aa6ade326d6342def4dafe7f37#body_text
is schema:about of	named entity 'ENCODED' named entity 'specificity' named entity 'cytomegalovirus' named entity 'activity' named entity 'Unique' named entity 'REVEALS' named entity 'SPECIFICITY' named entity 'PREVIOUSLY' named entity 'LEAD' named entity 'LARGE' named entity 'CLASS' named entity 'MODE' named entity 'THIOETHER LINKAGE' named entity 'CLASSIFY' named entity 'SUICIDE' named entity 'UNKNOWN' named entity 'UBIQUITIN' named entity 'HERPESVIRIDAE' named entity 'MEMBERS' named entity 'ACTIVITY' named entity 'MODULE' named entity 'INTERFACE' named entity 'UNIQUE' named entity 'CLASS' named entity 'CYSTEINE PROTEASE' named entity 'DEUBIQUITINATING' named entity 'CONTAIN' named entity 'REPORT' named entity 'LOOP' named entity 'DOMAIN' named entity 'DEUBIQUITINATING ENZYMES' named entity 'PROTEIN A' named entity 'BINDING' named entity 'FORMING' named entity 'CYSTEINE' named entity 'CRYSTAL STRUCTURE' named entity 'STRUCTURE' named entity 'COMPLEX' named entity 'THEIR' named entity 'ARTICLE' named entity 'HERPESVIRUS' named entity 'DEUBIQUITINATING ENZYMES' named entity 'ARRANGEMENT' named entity 'EXPOSED' named entity 'DISTINCT FROM' named entity 'ARCHITECTURE' named entity 'SUBSTRATE' named entity 'ACTIVE-SITE' named entity 'CYSTEINE PROTEASE' named entity 'OBSERVED' named entity 'EXTENSIVE' named entity 'LIKE' named entity 'PAPAIN' named entity 'USP' named entity 'CORE' named entity 'MURINE CYTOMEGALOVIRUS' named entity 'MEMBER OF' named entity 'M48' named entity 'TEGUMENT PROTEIN' named entity 'PROTEASE DOMAIN' named entity 'FOLD' named entity 'DISPLAYS' named entity 'HYDROPHOBIC INTERACTION' covid:arg/225ee16d130872aa6ade326d6342def4dafe7f37 named entity 'ubiquitin' named entity 'USP' named entity 'M48' named entity 'thioether' named entity 'binding' named entity 'substrate' named entity 'suicide' named entity 'Structure' named entity 'murine' named entity 'active-site' named entity 'protein' named entity 'suicide substrate'

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