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dc.contributor.authorMarshall, Stephen A.; orcid: 0000-0001-7678-4989; email: stephen.marshall@chem.ox.ac.uk
dc.contributor.authorPayne, Karl A. P.; orcid: 0000-0002-6331-6374
dc.contributor.authorFisher, Karl; orcid: 0000-0003-3539-8939
dc.contributor.authorTitchiner, Gabriel R.; orcid: 0000-0002-6378-9884
dc.contributor.authorLevy, Colin
dc.contributor.authorHay, Sam; orcid: 0000-0003-3274-0938
dc.contributor.authorLeys, David; orcid: 0000-0003-4845-8443; email: david.leys@manchester.ac.uk
dc.date.accessioned2021-08-20T15:39:56Z
dc.date.available2021-08-20T15:39:56Z
dc.date.issued2021-08-20
dc.date.submitted2020-12-03
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/625639/41467_2021_Article_25278.pdf?sequence=2
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/625639/additional-files.zip?sequence=3
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/625639/41467_2021_25278_MOESM6_ESM.pdf?sequence=4
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/625639/41467_2021_Article_25278_nlm.xml?sequence=5
dc.identifier.citationNature Communications, volume 12, issue 1, page 5065
dc.identifier.urihttp://hdl.handle.net/10034/625639
dc.descriptionFrom Springer Nature via Jisc Publications Router
dc.descriptionHistory: received 2020-12-03, accepted 2021-07-20, registration 2021-08-03, pub-electronic 2021-08-20, online 2021-08-20, collection 2021-12
dc.descriptionPublication status: Published
dc.descriptionFunder: EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council); doi: https://doi.org/10.13039/100010663; Grant(s): 695013
dc.descriptionFunder: RCUK | Biotechnology and Biological Sciences Research Council (BBSRC); doi: https://doi.org/10.13039/501100000268; Grant(s): BB/P000622/1
dc.description.abstractAbstract: The widespread UbiD enzyme family utilises the prFMN cofactor to achieve reversible decarboxylation of acrylic and (hetero)aromatic compounds. The reaction with acrylic compounds based on reversible 1,3-dipolar cycloaddition between substrate and prFMN occurs within the confines of the active site. In contrast, during aromatic acid decarboxylation, substantial rearrangement of the substrate aromatic moiety associated with covalent catalysis presents a molecular dynamic challenge. Here we determine the crystal structures of the multi-subunit vanillic acid decarboxylase VdcCD. We demonstrate that the small VdcD subunit acts as an allosteric activator of the UbiD-like VdcC. Comparison of distinct VdcCD structures reveals domain motion of the prFMN-binding domain directly affects active site architecture. Docking of substrate and prFMN-adduct species reveals active site reorganisation coupled to domain motion supports rearrangement of the substrate aromatic moiety. Together with kinetic solvent viscosity effects, this establishes prFMN covalent catalysis of aromatic (de)carboxylation is afforded by UbiD dynamics.
dc.languageen
dc.publisherNature Publishing Group UK
dc.rightsLicence for this article: http://creativecommons.org/licenses/by/4.0/
dc.sourceeissn: 2041-1723
dc.subjectArticle
dc.subject/631/45/535/1266
dc.subject/639/638/92/173
dc.subject/639/638/92/607
dc.subject/101
dc.subject/82/83
dc.subjectarticle
dc.titleUbiD domain dynamics underpins aromatic decarboxylation
dc.typearticle
dc.date.updated2021-08-20T15:39:56Z
dc.date.accepted2021-07-20


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