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dc.contributor.authorGarcia-Ferrer, Irene
dc.contributor.authorArêde, Pedro
dc.contributor.authorGómez-Blanco, Josué
dc.contributor.authorLuque, Daniel 
dc.contributor.authorDuquerroy, Stephane
dc.contributor.authorCastón, José R
dc.contributor.authorGoulas, Theodoros
dc.contributor.authorGomis-Rüth, F Xavier
dc.date.accessioned2020-05-08T12:37:07Z
dc.date.available2020-05-08T12:37:07Z
dc.date.issued2015-07-07
dc.identifier.citationProc Natl Acad Sci U S A. 2015 Jul 7;112(27):8290-5.es_ES
dc.identifier.issn0027-8424es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/9998
dc.description.abstractThe survival of commensal bacteria requires them to evade host peptidases. Gram-negative bacteria from the human gut microbiome encode a relative of the human endopeptidase inhibitor, α2-macroglobulin (α2M). Escherichia coli α2M (ECAM) is a ∼ 180-kDa multidomain membrane-anchored pan-peptidase inhibitor, which is cleaved by host endopeptidases in an accessible bait region. Structural studies by electron microscopy and crystallography reveal that this cleavage causes major structural rearrangement of more than half the 13-domain structure from a native to a compact induced form. It also exposes a reactive thioester bond, which covalently traps the peptidase. Subsequently, peptidase-laden ECAM is shed from the membrane and may dimerize. Trapped peptidases are still active except against very large substrates, so inhibition potentially prevents damage of large cell envelope components, but not host digestion. Mechanistically, these results document a novel monomeric "snap trap."es_ES
dc.language.isoenges_ES
dc.publisherNational Academy of Scienceses_ES
dc.relation.isversionofPublisher's versiones_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectX-ray crystal structurees_ES
dc.subjectconformational rearrangementes_ES
dc.subjectcryo-electron microscopyes_ES
dc.subjectgut microbiomees_ES
dc.subjectprotein inhibitores_ES
dc.subject.meshAmino Acid Sequence es_ES
dc.subject.meshBinding Sites es_ES
dc.subject.meshCrystallography, X-Ray es_ES
dc.subject.meshEndopeptidases es_ES
dc.subject.meshEscherichia coli es_ES
dc.subject.meshEscherichia coli Proteins es_ES
dc.subject.meshGastrointestinal Tract es_ES
dc.subject.meshHumans es_ES
dc.subject.meshMembrane Proteins es_ES
dc.subject.meshMicrobiota es_ES
dc.subject.meshMicroscopy, Electron es_ES
dc.subject.meshModels, Moleculares_ES
dc.subject.meshMolecular Sequence Data es_ES
dc.subject.meshMolecular Weight es_ES
dc.subject.meshPeptide Hydrolases es_ES
dc.subject.meshProtease Inhibitors es_ES
dc.subject.meshProtein Multimerization es_ES
dc.subject.meshProtein Structure, Secondary es_ES
dc.subject.meshProtein Structure, Tertiaryes_ES
dc.subject.meshalpha-Macroglobulins es_ES
dc.titleStructural and functional insights into Escherichia coli α2-macroglobulin endopeptidase snap-trap inhibitiones_ES
dc.typeArtículoes_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.identifier.pubmedID26100869es_ES
dc.format.volume112es_ES
dc.format.number27es_ES
dc.format.page8290-5es_ES
dc.identifier.doi10.1073/pnas.1506538112es_ES
dc.description.peerreviewedes_ES
dc.identifier.e-issn1091-6490es_ES
dc.relation.publisherversionhttps://doi.org/10.1073/pnas.1506538112es_ES
dc.identifier.journalProceedings of the National Academy of Sciences of the United States of Americaes_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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Atribución-NoComercial-CompartirIgual 4.0 Internacional
This item is licensed under a: Atribución-NoComercial-CompartirIgual 4.0 Internacional