Mostra el registre parcial de l'element

dc.contributorUniversitat Ramon Llull. IQS
dc.contributor.authorFaijes, Magda
dc.contributor.authorVal Cid, Cristina
dc.contributor.authorBiarnés Fontal, Xevi
dc.contributor.authorPlanas, Antoni (Planas Sauter)
dc.date.accessioned2021-01-18T13:27:03Z
dc.date.accessioned2023-07-13T05:43:31Z
dc.date.available2021-01-18T13:27:03Z
dc.date.available2023-07-13T05:43:31Z
dc.date.issued2015-05
dc.identifier.urihttp://hdl.handle.net/20.500.14342/971
dc.description.abstractHexosaminidases are involved in important biological processes catalyzing the hydrolysis of N-acetyl-hexosaminyl residues in glycosaminoglycans and glycoconjugates. The GH20 enzymes present diverse domain organizations for which we propose two minimal model architectures: Model A containing at least a non-catalytic GH20b domain and the catalytic one (GH20) always accompanied with an extra α-helix (GH20b-GH20-α), and Model B with only the catalytic GH20 domain. The large Bifidobacterium bifidum lacto-N-biosidase was used as a model protein to evaluate the minimal functional unit due to its interest and structural complexity. By expressing different truncated forms of this enzyme, we show that Model A architectures cannot be reduced to Model B. In particular, there are two structural requirements general to GH20 enzymes with Model A architecture. First, the non-catalytic domain GH20b at the N-terminus of the catalytic GH20 domain is required for expression and seems to stabilize it. Second, the substrate-binding cavity at the GH20 domain always involves a remote element provided by a long loop from the catalytic domain itself or, when this loop is short, by an element from another domain of the multidomain structure or from the dimeric partner. Particularly, the lacto-N-biosidase requires GH20b and the lectin-like domain at the N- and C-termini of the catalytic GH20 domain to be fully soluble and functional. The lectin domain provides this remote element to the active site. We demonstrate restoration of activity of the inactive GH20b-GH20-α construct (model A architecture) by a complementation assay with the lectin-like domain. The engineering of minimal functional units of multidomain GH20 enzymes must consider these structural requirements.eng
dc.format.extent17 p.cat
dc.language.isoengcat
dc.publisherPublic Library of Science (PLoS)cat
dc.relation.ispartofPLoS ONE. Vol.10, n.5 (2015), e0128075cat
dc.rightsAttribution 4.0 International
dc.rights© L'autor/a
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.sourceRECERCAT (Dipòsit de la Recerca de Catalunya)
dc.subject.otherEnzimscat
dc.subject.otherProteïnescat
dc.subject.otherLectinescat
dc.subject.otherProteïnes--Estructuracat
dc.subject.otherCristallscat
dc.subject.otherProtein domainscat
dc.subject.otherProtein structurecat
dc.subject.otherProtein structure databasescat
dc.subject.otherEnzyme structurecat
dc.subject.otherEnzymescat
dc.subject.otherLectinscat
dc.subject.otherCrystal structurecat
dc.subject.otherArgininecat
dc.titleStructural-functional analysis reveals a specific domain organization in family GH20 hexosaminidasescat
dc.typeinfo:eu-repo/semantics/articlecat
dc.typeinfo:eu-repo/semantics/publishedVersioncat
dc.rights.accessLevelinfo:eu-repo/semantics/openAccess
dc.embargo.termscapcat
dc.subject.udc577
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0128075cat
dc.relation.projectIDinfo:eu-repo/grantAgreement/EC/FP7/FP7-KBBE-2013-7cat
dc.relation.projectIDinfo:eu-repo/grantAgreement/EU/H2020/Grant No. 613931cat
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO/PN I+D/BIO2013-49022-C2-1-Rcat


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Mostra el registre parcial de l'element

Attribution 4.0 International
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