Molecular Mechanisms of Yeast Cell Wall Glucan Remodeling
| Autor: | Isabelle Mouyna, Thierry Fontaine, Adel F. M. Ibrahim, Sharon M. Shepherd, Jean-Paul Latgé, Ramon Hurtado-Guerrero, Daan M. F. van Aalten, Alexander W. Schüttelkopf |
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| Přispěvatelé: | University of Dundee, Aspergillus, Institut Pasteur [Paris] (IP), This work was supported by a Wellcome Trust senior research fellowship (to D. M. F. v. A.) and European Union FP6 STREP Fungwall Programme., European Project: 511952,FUNGWALL(2005), Institut Pasteur [Paris] |
| Rok vydání: | 2009 |
| Předmět: |
Protein Folding
Saccharomyces cerevisiae Proteins MESH: Protein Folding Saccharomyces cerevisiae Glycobiology and Extracellular Matrices Crystallography X-Ray Biochemistry MESH: Protein Structure Tertiary 03 medical and health sciences Hydrolysis MESH: Cell Wall MESH: Saccharomyces cerevisiae Proteins Cell Wall MESH: Glucans Glycosyltransferase Glycoside hydrolase Glucans Molecular Biology [SDV.MP.MYC]Life Sciences [q-bio]/Microbiology and Parasitology/Mycology 030304 developmental biology Glucan chemistry.chemical_classification 0303 health sciences biology 030306 microbiology Glucan Endo-1 3-beta-D-Glucosidase Cell Biology MESH: Crystallography X-Ray biology.organism_classification MESH: Glucan Endo-1 3-beta-D-Glucosidase MESH: Saccharomyces cerevisiae Yeast Protein Structure Tertiary Enzyme chemistry biology.protein Binding domain |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, 2009, 284 (13), pp.8461-8469. ⟨10.1074/jbc.M807990200⟩ Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (13), pp.8461-8469. ⟨10.1074/jbc.M807990200⟩ |
| ISSN: | 0021-9258 1083-351X |
| DOI: | 10.1074/jbc.m807990200 |
| Popis: | International audience; Yeast cell wall remodeling is controlled by the equilibrium between glycoside hydrolases, glycosyltransferases, and transglycosylases. Family 72 glycoside hydrolases (GH72) are ubiquitous in fungal organisms and are known to possess significant transglycosylase activity, producing elongated beta(1-3) glucan chains. However, the molecular mechanisms that control the balance between hydrolysis and transglycosylation in these enzymes are not understood. Here we present the first crystal structure of a glucan transglycosylase, Saccharomyces cerevisiae Gas2 (ScGas2), revealing a multidomain fold, with a (betaalpha)(8) catalytic core and a separate glucan binding domain with an elongated, conserved glucan binding groove. Structures of ScGas2 complexes with different beta-glucan substrate/product oligosaccharides provide "snapshots" of substrate binding and hydrolysis/transglycosylation giving the first insights into the mechanisms these enzymes employ to drive beta(1-3) glucan elongation. Together with mutagenesis and analysis of reaction products, the structures suggest a "base occlusion" mechanism through which these enzymes protect the covalent protein-enzyme intermediate from a water nucleophile, thus controlling the balance between hydrolysis and transglycosylation and driving the elongation of beta(1-3) glucan chains in the yeast cell wall. |
| Databáze: | OpenAIRE |
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