About: Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members

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About: Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members Goto Sponge NotDistinct Permalink

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

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members
Creator	Bonis, Mathilde Haouz, Ahmed Michaud, Yann Raynal, Bertrand Taha, Muhamed-Kheir Boneca, Ivo Veyrier, Frédéric White, Stephen Williams, Allison
Source	Medline; PMC
abstract	Peptidoglycan O-acetylesterase (Ape1), which is required for host survival in Neisseria sp., belongs to the diverse SGNH hydrolase superfamily, which includes important viral and bacterial virulence factors. Here, multi-domain crystal structures of Ape1 with an SGNH catalytic domain and a newly identified putative peptidoglycan-detection module are reported. Enzyme catalysis was performed in Ape1 crystals and key catalytic intermediates along the SGNH esterase hydrolysis reaction pathway were visualized, revealing a substrate-induced productive conformation of the catalytic triad, a mechanistic detail that has not previously been observed. This substrate-induced productive conformation of the catalytic triad shifts the established dogma on these enzymes, generating valuable insight into the structure-based design of drugs targeting the SGNH esterase superfamily.
has issue date	2014-09-27(xsd:dateTime)
bibo:doi	10.1107/s1399004714016770
bibo:pmid	25286847
has license	cc-by
sha1sum (hex)	d7817865765ddf7b0e1635e74b7a9393d0979a66
schema:url	https://doi.org/10.1107/s1399004714016770
resource representing a document's title	Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members
has PubMed Central identifier	PMC4188005
has PubMed identifier	25286847
schema:publication	Acta Crystallogr D Biol Crystallogr
resource representing a document's body	covid:d7817865765ddf7b0e1635e74b7a9393d0979a66#body_text
is schema:about of	named entity 'dogma' named entity 'catalytic triad' named entity 'enzymes' named entity 'ESTERASE' covid:arg/d7817865765ddf7b0e1635e74b7a9393d0979a66 named entity 'INDUCED' named entity 'PEPTIDOGLYCAN' named entity 'GENERATING' named entity 'INSIGHT' named entity 'BACTERIAL VIRULENCE' named entity 'DIVERSE' named entity 'NEISSERIA SP.' named entity 'IDENTIFIED' named entity 'ESTERASE' named entity 'REQUIRED' named entity 'REACTION' named entity 'CONFORMATION' named entity 'INCLUDES' named entity 'DETECTION' named entity 'APE1' named entity 'INTERMEDIATES' named entity 'ENZYME' named entity 'PREVIOUSLY' named entity 'HYDROLASE' named entity 'REVEALING' named entity 'DRUGS TARGETING' named entity 'HOST' named entity 'SUBSTRATE' named entity 'CATALYTIC DOMAIN' named entity 'STRUCTURE' named entity 'THESE' named entity 'DOMAIN' named entity 'VISUALIZED' named entity 'CRYSTAL' named entity 'HERE' named entity 'FAMILY MEMBERS' named entity 'CRYSTALLOGRAPHY' named entity 'SURVIVAL' named entity 'MODULE' named entity 'VIRULENCE FACTORS' named entity 'ACETYLESTERASE' named entity 'PRODUCTIVE' named entity 'PEPTIDOGLYCAN' named entity 'SUBSTRATE' named entity 'BIOLOGICAL' named entity 'CONFORMATION' named entity 'CATALYTIC TRIAD' named entity 'CONSERVATION' named entity 'REPORTED' named entity 'NEWLY' named entity 'STRUCTURES' named entity 'PATHWAY' named entity 'SUPERFAMILY' named entity 'VIRAL AND' named entity 'CRYSTALS' named entity 'IMPORTANT' named entity 'BASED' named entity 'SHIFTS' named entity 'OBSERVED' named entity 'ESTABLISHED' named entity 'DESIGN' named entity 'INDUCED' named entity 'ACETYLESTERASE' named entity 'PRODUCTIVE' named entity 'VISUALIZATION' named entity 'REVEALS' named entity 'HYDROLYSIS' named entity 'KEY' named entity 'CATALYTIC TRIAD' named entity 'NEISSERIA MENINGITIDIS' named entity 'PERFORMED' named entity 'ENZYMES' named entity 'MULTI'

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