6F1J

Structure of a Talaromyces pinophilus GH62 Arabinofuranosidase in complex with AraDNJ at 1.25A resolution

Summary for 6F1J

• Entry DOI: 10.2210/pdb6f1j/pdb
• Descriptor: protein, 1,4-DIDEOXY-1,4-IMINO-L-ARABINITOL, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: biofuels, glycosidase, enzyme, enzyme inhibitor, sugar binding protein, hydrolase
• Biological source: Talaromyces pinophilus
• Total number of polymer chains: 2
• Total formula weight: 70167.94

Authors

Moroz, O.V.,Sobala, L.,Blagova, E.,Coyle, T.,Morkeberg Krogh, K.B.R.,Wei, P.,Stubbs, K.,Wilson, K.S.,Davies, G.J. (deposition date: 2017-11-22, release date: 2018-08-15, Last modification date: 2024-11-06)

Primary citation

Moroz, O.V.,Sobala, L.F.,Blagova, E.,Coyle, T.,Peng, W.,Morkeberg Krogh, K.B.R.,Stubbs, K.A.,Wilson, K.S.,Davies, G.J.
Structure of a Talaromyces pinophilus GH62 arabinofuranosidase in complex with AraDNJ at 1.25 angstrom resolution.
Acta Crystallogr F Struct Biol Commun, 74:490-495, 2018

PubMed 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 K 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.

PubMed: 30084398
DOI: 10.1107/S2053230X18000250

Experimental method

X-RAY DIFFRACTION (1.25 Å)