Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site

Vista sencilla de ítem
dc.contributor.authorStreltsov, Victor A.
dc.contributor.authorLuang, Sukanya
dc.contributor.authorPeisley, Alys
dc.contributor.authorVarghese, Joseph N.
dc.contributor.authorKetudat Cairns, James R.
dc.contributor.authorFort, Sebastien
dc.contributor.authorHijnen, Marcel
dc.contributor.authorTvaroška, Igor
dc.contributor.authorArda, Ana
dc.contributor.authorJiménez-Barbero, Jesús
dc.contributor.authorAlfonso-Prieto, Mercedes
dc.contributor.authorRovira, Carme
dc.contributor.authorMendoza, Fernanda
dc.contributor.authorTiessler-Sala, Laura
dc.contributor.authorSánchez-Aparicio, José-Emilio
dc.contributor.authorRodríguez-Guerra, Jaime
dc.contributor.authorM. Lluch, José
dc.contributor.authorMaréchal, Jean-Didier
dc.contributor.authorMasgrau, Laura
dc.contributor.authorHrmova, Maria
dc.date.accessioned2021-09-15T13:45:46Z
dc.date.available2021-09-15T13:45:46Z
dc.date.issued2019-12
dc.descriptionIndexación: Scopues
dc.description.abstractSubstrates associate and products dissociate from enzyme catalytic sites rapidly, which hampers investigations of their trajectories. The high-resolution structure of the native Hordeum exo-hydrolase HvExoI isolated from seedlings reveals that non-covalently trapped glucose forms a stable enzyme-product complex. Here, we report that the alkyl β-d-glucoside and methyl 6-thio-β-gentiobioside substrate analogues perfused in crystalline HvExoI bind across the catalytic site after they displace glucose, while methyl 2-thio-β-sophoroside attaches nearby. Structural analyses and multi-scale molecular modelling of nanoscale reactant movements in HvExoI reveal that upon productive binding of incoming substrates, the glucose product modifies its binding patterns and evokes the formation of a transient lateral cavity, which serves as a conduit for glucose departure to allow for the next catalytic round. This path enables substrate-product assisted processive catalysis through multiple hydrolytic events without HvExoI losing contact with oligo- or polymeric substrates. We anticipate that such enzyme plasticity could be prevalent among exo-hydrolases. © 2019, Crown.es
dc.description.urihttps://www-nature-com.recursosbiblioteca.unab.cl/articles/s41467-019-09691-z
dc.identifier.citationNature Communications Volume 10, Issue 11 December 2019 Article number 2222es
dc.identifier.doi10.1038/s41467-019-09691-z
dc.identifier.issn2041-1723
dc.identifier.urihttp://repositorio.unab.cl/xmlui/handle/ria/20270
dc.language.isoenes
dc.publisherNature Publishing Groupes
dc.rights.licenseAtribución 4.0 Internacional (CC BY 4.0)
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/deed.es
dc.subjectBiocatalysises
dc.subjectCatalytic Domaines
dc.subjectCrystallography, X-Rayes
dc.subjectEnzyme Assayses
dc.subjectGlucosidaseses
dc.subjectGlycosideses
dc.subjectHordeumes
dc.subjectModels, Moleculares
dc.subjectMolecular Dynamics Simulationes
dc.subjectNuclear Magnetic Resonance, Biomoleculares
dc.subjectPlant Proteinses
dc.subjectRecombinant Proteinses
dc.subjectSeedlingses
dc.subjectSubstrate Specificityes
dc.titleDiscovery of processive catalysis by an exo-hydrolase with a pocket-shaped active sitees
dc.typeArtículoes
Archivos
Bloque original
Mostrando 1 - 1 de 1
Miniatura
Nombre:
s41467-019-09691-z.pdf
Tamaño:
4.26 MB
Formato:
Adobe Portable Document Format
Descripción:
TEXTO COMPLETO EN INGLES
Descargar
Bloque de licencias
Mostrando 1 - 1 de 1
No hay miniatura disponible
Nombre:
license.txt
Tamaño:
1.71 KB
Formato:
Item-specific license agreed upon to submission
Descripción:
Descargar
Colecciones
FCE - Artículos de Revista