NDLI: First structural insights into -L-arabinofuranosidases from the two GH62 glycoside hydrolase subfamilies.

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First structural insights into -L-arabinofuranosidases from the two GH62 glycoside hydrolase subfamilies.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Burlet-schiltz, Odile Marcellin, Marlène Coutinho, Pedro M. Henrissat, Bernard Siguier, Béatrice O'donohue, Michael J. Haon, Mireille Tranier, Samuel Nahoum, Virginie Mourey, Lionel Berrin, Jean-guy Dumon, Claire
Description	Author Affiliation: Siguier B ( From the Université de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse.)
Abstract	-L-arabinofuranosidases are glycoside hydrolases that specifically hydrolyze non-reducing residues from arabinose-containing polysaccharides. In the case of arabinoxylans, which are the main components of hemicellulose, they are part of microbial xylanolytic systems and are necessary for complete breakdown of arabinoxylans. Glycoside hydrolase family 62 (GH62) is currently a small family of -L-arabinofuranosidases that contains only bacterial and fungal members. Little is known about the GH62 mechanism of action, because only a few members have been biochemically characterized and no three-dimensional structure is available. Here, we present the first crystal structures of two fungal GH62 -L-arabinofuranosidases from the basidiomycete Ustilago maydis (UmAbf62A) and ascomycete Podospora anserina (PaAbf62A). Both enzymes are able to efficiently remove the -L-arabinosyl substituents from arabinoxylan. The overall three-dimensional structure of UmAbf62A and PaAbf62A reveals a five-bladed ß-propeller fold that confirms their predicted classification into clan GH-F together with GH43 -L-arabinofuranosidases. Crystallographic structures of the complexes with arabinose and cellotriose reveal the important role of subsites +1 and +2 for sugar binding. Intriguingly, we observed that PaAbf62A was inhibited by cello-oligosaccharides and displayed binding affinity to cellulose although no activity was observed on a range of cellulosic substrates. Bioinformatic analyses showed that UmAbf62A and PaAbf62A belong to two distinct subfamilies within the GH62 family. The results presented here provide a framework to better investigate the structure-function relationships within the GH62 family.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	8
Volume Number	289
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2014-02-21
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Fungal Proteins Chemistry Glycoside Hydrolases Multigene Family Podospora Enzymology Ustilago Arabinose Metabolism Calorimetry Catalytic Domain Cellulose Crystallography, X-Ray Kinetics Models, Molecular Phylogeny Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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