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Structure of a Talaromyces pinophilus GH62 arabinofuranosidase in complex with AraDNJ at 1.25 Å resolution
DOI:
10.1107/S2053230X18000250
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
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
Diamond Keywords: Fungi; Biofuel; Enzymes
Subject Areas:
Biology and Bio-materials,
Energy,
Chemistry
Instruments:
I04-Macromolecular Crystallography
Added On:
31/07/2018 10:50
Documents:
va5006.pdf
Discipline Tags:
Bioenergy
Earth Sciences & Environment
Sustainable Energy Systems
Energy
Climate Change
Biochemistry
Catalysis
Chemistry
Structural biology
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)