Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism

dc.contributor.authorLiberato, Marcelo V.
dc.contributor.authorSilveira, Rodrigo L.
dc.contributor.authorPrates, Erica T.
dc.contributor.authorAraujo, Evandro A. de
dc.contributor.authorPellegrini, Vanessa O. A.
dc.contributor.authorCamilo, Cesar M.
dc.contributor.authorKadowaki, Marco A.
dc.contributor.authorNeto, Mario de O. [UNESP]
dc.contributor.authorPopov, Alexander
dc.contributor.authorSkaf, Munir S.
dc.contributor.authorPolikarpov, Igor
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionEuropean Synchrotron Radiat Facil
dc.date.accessioned2018-11-26T15:29:11Z
dc.date.available2018-11-26T15:29:11Z
dc.date.issued2016-04-01
dc.description.abstractGlycoside hydrolases (GHs) play fundamental roles in the decomposition of lignocellulosic biomaterials. Here, we report the full-length structure of a cellulase from Bacillus licheniformis (BlCel5B), a member of the GH5 subfamily 4 that is entirely dependent on its two ancillary modules (Ig-like module and CBM46) for catalytic activity. Using X-ray crystallography, small-angle X-ray scattering and molecular dynamics simulations, we propose that the C-terminal CBM46 caps the distal N-terminal catalytic domain (CD) to establish a fully functional active site via a combination of large-scale multidomain conformational selection and induced-fit mechanisms. The Ig-like module is pivoting the packing and unpacking motions of CBM46 relative to CD in the assembly of the binding subsite. This is the first example of a multidomain GH relying on large amplitude motions of the CBM46 for assembly of the catalytically competent form of the enzyme.en
dc.description.affiliationUniv Sao Paulo, Sao Carlos Inst Phys, BR-13566590 Sao Paulo, Brazil
dc.description.affiliationUniv Estadual Campinas, Inst Chem, BR-13084862 Sao Paulo, Brazil
dc.description.affiliationState Univ Sao Paulo, Inst Biosci, BR-18618970 Sao Paulo, Brazil
dc.description.affiliationEuropean Synchrotron Radiat Facil, CS40220, Grenoble, France
dc.description.affiliationUnespState Univ Sao Paulo, Inst Biosci, BR-18618970 Sao Paulo, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipIdFAPESP: 2008/56255-9
dc.description.sponsorshipIdFAPESP: 2009/52840-7
dc.description.sponsorshipIdFAPESP: 2010/18773-8
dc.description.sponsorshipIdFAPESP: 2013/08293-7
dc.description.sponsorshipIdFAPESP: 2013/15582-5
dc.description.sponsorshipIdFAPESP: 2014/10448-1
dc.description.sponsorshipIdCNPq: 490022/2009-0
dc.description.sponsorshipIdCNPq: 301981/2011-6
dc.description.sponsorshipIdCNPq: 500091/2014-5
dc.description.sponsorshipIdCNPq: 310177/2011-1
dc.format.extent15
dc.identifierhttp://dx.doi.org/10.1038/srep23473
dc.identifier.citationScientific Reports. London: Nature Publishing Group, v. 6, 15 p., 2016.
dc.identifier.doi10.1038/srep23473
dc.identifier.fileWOS000373302600001.pdf
dc.identifier.issn2045-2322
dc.identifier.urihttp://hdl.handle.net/11449/158786
dc.identifier.wosWOS:000373302600001
dc.language.isoeng
dc.publisherNature Publishing Group
dc.relation.ispartofScientific Reports
dc.relation.ispartofsjr1,533
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.titleMolecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanismen
dc.typeArtigo
dcterms.rightsHolderNature Publishing Group
unesp.author.orcid0000-0002-3058-8912[9]
unesp.author.orcid0000-0001-9496-4174[11]

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