Secondary structure reshuffling modulates glycosyltransferase function at the membrane
| Autor: | Marco Bellinzoni, Alexandre Chenal, David Albesa-Jové, Natalia Comino, David Giganti, Mariano A. Martinez, Marcelo E. Guerin, Saioa Urresti, Ane Rodrigo-Unzueta, Nathalie Barilone, Pedro M. Alzari |
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| Přispěvatelé: | Departamento de Bioquimica, Universidad del Pais Vasco / Euskal Herriko Unibertsitatea [Espagne] (UPV/EHU), Microbiologie structurale - Structural Microbiology (Microb. Struc. (UMR_3528 / U-Pasteur_5)), Université Paris Diderot - Paris 7 (UPD7)-Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Unidad de Biofísica, Centro Mixto Consejo Superior de Investigaciones Científicas-Universidad del País Vasco/Euskal Herriko Unibertsitatea (SIC, UPV/EHU), Biochimie des Interactions Macromoléculaires / Biochemistry of Macromolecular Interactions, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), IKERBASQUE, IKERBASQUE, Basque Foundation for Science, 48011, Bilbao, Spain, This work was supported by the European Community’s Sixth and Seventh Framework Programmes (contracts LSHP-CT-2005-018923 and HEALTH-F3-2011-260872), the Institut Pasteur, the Spanish Ministry of Science and Innovation (contracts SAF2010-19096 and BIO2013-49022-C2-2-R), IKERBASQUE, the Basque Foundation for Science, the Basque Government and the Fundación Biofísica Bizkaia., European Project: LSHP-CT, Institut Pasteur [Paris] (IP)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), University of the Basque Country/Euskal Herriko Unibertsitatea (UPV/EHU), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Ikerbasque - Basque Foundation for Science, Institut Pasteur [Paris]-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Biochimie des Interactions Macromoléculaires |
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Mannosyltransferase Crystallography X-Ray Mannosyltransferases Protein Structure Secondary MESH: Cell Membrane/enzymology/metabolism Protein structure Bacterial Proteins Glycosyltransferase MESH: Glycosyltransferases/metabolism Animals Humans Transferase MESH: Animals [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Molecular Biology Protein secondary structure Phospholipids biology Cell Membrane Glycosyltransferases Cell Biology MESH: Crystallography X-Ray MESH: Bacterial Proteins/chemistry/genetics MESH: isolation & purification Membrane Biochemistry Catalytic cycle Mutagenesis Site-Directed Biophysics biology.protein Function (biology) |
| Zdroj: | Nature Chemical Biology Nature Chemical Biology, Nature Publishing Group, 2014, 11 (1), pp.16-18. ⟨10.1038/nchembio.1694⟩ Nature Chemical Biology, 2014, 11 (1), pp.16-18. ⟨10.1038/nchembio.1694⟩ |
| ISSN: | 1552-4450 1552-4469 |
| DOI: | 10.1038/nchembio.1694⟩ |
| Popis: | International audience; Secondary structure refolding is a key event in biology as it modulates the conformation of many proteins in the cell, generating functional or aberrant states. The crystal structures of mannosyltransferase PimA reveal an exceptional flexibility of the protein along the catalytic cycle, including β-strand-to-α-helix and α-helix-to-β-strand transitions. These structural changes modulate catalysis and are promoted by interactions of the protein with anionic phospholipids in the membrane. |
| Databáze: | OpenAIRE |
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