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Structure of a Talaromyces pinophilus GH62 arabinofuranosidase in complex with AraDNJ at 1.25 Å resolution

DOI: 10.1107/S2053230X18000250 DOI Help

Authors: Olga V. Moroz (The University of York) , Lukasz F. Sobala (The University of York) , Elena Blagova (The University of York) , Travis Coyle (The University of Western Australia) , Wei Peng (Novozymes A/S) , Kristian B. R. Mørkeberg Krogh (Novozymes A/S) , Keith A. Stubbs (The University of Western Australia) , Keith S. Wilson (The University of York) , Gideon J. Davies (The University of York)
Co-authored by industrial partner: Yes

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 74

State: Published (Approved)
Published: August 2018
Diamond Proposal Number(s): 13587

Open Access Open Access

Abstract: The enzymatic hydrolysis of complex plant biomass is a major societal goal of the 21st century in order to deliver renewable energy from nonpetroleum and nonfood sources. One of the major problems in many industrial processes, including the production of second-generation biofuels from lignocellulose, is the presence of `hemicelluloses' such as xylans which block access to the cellulosic biomass. Xylans, with a polymeric β-1,4-xylose backbone, are frequently decorated with acetyl, glucuronyl and arabinofuranosyl `side-chain' substituents, all of which need to be removed for complete degradation of the xylan. As such, there is interest in side-chain-cleaving enzymes and their action on polymeric substrates. Here, the 1.25 Å resolution structure of the Talaromyces pinophilus arabinofuranosidase in complex with the inhibitor AraDNJ, which binds with a Kd of 24 ± 0.4 µM, is reported. Positively charged iminosugars are generally considered to be potent inhibitors of retaining glycosidases by virtue of their ability to interact with both acid/base and nucleophilic carboxylates. Here, AraDNJ shows good inhibition of an inverting enzyme, allowing further insight into the structural basis for arabinoxylan recognition and degradation.

Journal Keywords: biofuels; glycosidases; enzymes; enzyme inhibitors; Talaromyces pinophilus; arabinofuranosidase

Subject Areas: Biology and Bio-materials, Energy

Instruments: I04-Macromolecular Crystallography