title: Structural and biochemical analyses of glycoside hydrolase families 5 and 26 β-(1,4)-mannanases from Podospora anserina reveal differences upon manno-oligosaccharide catalysis.
abstract: The microbial deconstruction of the plant cell wall is a key biological process that is of increasing importance with the development of a sustainable biofuel industry. The glycoside hydrolase families GH5 (PaMan5A) and GH26 (PaMan26A) endo-β-1,4-mannanases from the coprophilic ascomycete Podospora anserina contribute to the enzymatic degradation of lignocellulosic biomass. In this study, P. anserina mannanases were further subjected to detailed comparative analysis of their substrate specificities, active site organization, and transglycosylation capacity. Although PaMan5A displays a classical mode of action, PaMan26A revealed an atypical hydrolysis pattern with the release of mannotetraose and mannose from mannopentaose resulting from a predominant binding mode involving the -4 subsite. The crystal structures of PaMan5A and PaMan26A were solved at 1.4 and 2.85 Å resolution, respectively. Analysis of the PaMan26A structure supported strong interaction with substrate at the -4 subsite mediated by two aromatic residues Trp-244 and Trp-245. The PaMan26A structure appended to its family 35 carbohydrate binding module revealed a short and proline-rich rigid linker that anchored together the catalytic and the binding modules.
authors.affiliation: INRA, UMR1163 BCF, Aix Marseille Université, Polytech Marseille, F-13288 Marseille, France.
authors.forename: Marie
authors.initials: M
authors.lastname: Couturier
authors.affiliation: Architecture et Fonction des Macromolécules Biologiques, Aix Marseille Université, CNRS UMR7257, F-13288 Marseille, France.
authors.forename: Alain
authors.initials: A
authors.lastname: Roussel
authors.affiliation: Department of Biochemistry and Structural Biology, Lund University, P. O. Box 124, S-221 00, Lund, Sweden.
authors.forename: Anna
authors.initials: A
authors.lastname: Rosengren
authors.affiliation: Architecture et Fonction des Macromolécules Biologiques, Aix Marseille Université, CNRS UMR7257, F-13288 Marseille, France.
authors.forename: Philippe
authors.initials: P
authors.lastname: Leone
authors.affiliation: Department of Biochemistry and Structural Biology, Lund University, P. O. Box 124, S-221 00, Lund, Sweden.
authors.forename: Henrik
authors.initials: H
authors.lastname: Stålbrand
authors.affiliation: INRA, UMR1163 BCF, Aix Marseille Université, Polytech Marseille, F-13288 Marseille, France. Electronic address: jean-guy.berrin@univ-amu.fr.
authors.forename: Jean-Guy
authors.initials: JG
authors.lastname: Berrin
mesh_terms: D002384:Catalysis; D020134:Catalytic Domain; D002473:Cell Wall / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics; D006031:Glycosylation; D006868:Hydrolysis; D016296:Mutagenesis; D009844:Oligosaccharides / Q000737:chemistry*; D048468:Podospora / Q000201:enzymology*; D011134:Polysaccharides / Q000737:chemistry; D011392:Proline / Q000737:chemistry; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
chemical_list: D009844:Oligosaccharides; D011134:Polysaccharides; D011392:Proline; D006026:Glycoside Hydrolases
keywords: CAZymes; Carbohydrate; Enzyme Structure; Fungi; Glycoside Hydrolases; Mannan; Plant Cell Wall; Polysaccharide
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