Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism
| العنوان: | Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism |
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| المؤلفون: | Erica T. Prates, Evandro Ares de Araújo, Mario de Oliveira Neto, Rodrigo L. Silveira, Alexander Popov, Munir S. Skaf, Igor Polikarpov, Vanessa de Oliveira Arnoldi Pellegrini, Cesar M. Camilo, Marco Antonio Seiki Kadowaki, Marcelo Vizoná Liberato |
| المساهمون: | Universidade de São Paulo (USP), Universidade Estadual de Campinas (UNICAMP), Universidade Estadual Paulista (Unesp), European Synchrotron Radiat Facil, Univ Sao Paulo, Sao Carlos Inst Phys, BR-13566590 Sao Paulo, Brazil, Univ Estadual Campinas, Inst Chem, BR-13084862 Sao Paulo, Brazil, State Univ Sao Paulo, Inst Biosci, BR-18618970 Sao Paulo, Brazil, European Synchrotron Radiation Facility (ESRF) |
| المصدر: | Web of Science Repositório Institucional da UNESP Universidade Estadual Paulista (UNESP) instacron:UNESP 'Scientific Reports ', vol: 6, pages: 23473-1-23473-15 (2016) Scientific Reports Scientific Reports, Nature Publishing Group, 2016, 6, 15 p. ⟨10.1038/srep23473⟩ Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP |
| بيانات النشر: | Nature Publishing Group, 2016. |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | 0301 basic medicine, Models, Molecular, Subfamily, Stereochemistry, Protein Conformation, [SDV]Life Sciences [q-bio], Cellulase, Biology, Molecular Dynamics Simulation, Crystallography, X-Ray, 01 natural sciences, Article, Substrate Specificity, 03 medical and health sciences, Molecular dynamics, Motion, Bacterial Proteins, Protein Domains, X-Ray Diffraction, Catalytic Domain, 0103 physical sciences, Hydrolase, Consensus Sequence, Scattering, Small Angle, Bacillus licheniformis, Glycoside hydrolase, Amino Acid Sequence, Cellulose, Phylogeny, chemistry.chemical_classification, Genetics, Multidisciplinary, Binding Sites, 010304 chemical physics, Sequence Homology, Amino Acid, Active site, MICROBIOLOGIA, biology.organism_classification, Corrigenda, Recombinant Proteins, 030104 developmental biology, Enzyme, chemistry, biology.protein, Mutagenesis, Site-Directed, Tetroses, Sequence Alignment |
| الوصف: | Made available in DSpace on 2018-11-26T15:29:11Z (GMT). No. of bitstreams: 0 Previous issue date: 2016-04-01 Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Glycoside 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. Univ Sao Paulo, Sao Carlos Inst Phys, BR-13566590 Sao Paulo, Brazil Univ Estadual Campinas, Inst Chem, BR-13084862 Sao Paulo, Brazil State Univ Sao Paulo, Inst Biosci, BR-18618970 Sao Paulo, Brazil European Synchrotron Radiat Facil, CS40220, Grenoble, France State Univ Sao Paulo, Inst Biosci, BR-18618970 Sao Paulo, Brazil FAPESP: 2008/56255-9 FAPESP: 2009/52840-7 FAPESP: 2010/18773-8 FAPESP: 2013/08293-7 FAPESP: 2013/15582-5 FAPESP: 2014/10448-1 CNPq: 490022/2009-0 CNPq: 301981/2011-6 CNPq: 500091/2014-5 CNPq: 310177/2011-1 |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 2045-2322 |
| DOI: | 10.1038/srep23473⟩ |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4466b9725835f27d2f8e5dfbd2622aa9 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....4466b9725835f27d2f8e5dfbd2622aa9 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 20452322 |
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| DOI: | 10.1038/srep23473⟩ |