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The three-dimensional structure of the cellobiohydrolase Cel7A from Aspergillus fumigatus at 1.5 Å resolution

DOI: 10.1107/S2053230X14027307 DOI Help
PMID: 25615982 PMID Help

Authors: Olga Moroz (University of York) , Michelle Maranta (Novozymes Inc.,shaghasi) , Tarana Shaghasi (Novozymes Inc.,) , Paul V. Harris (Novozymes Inc.,) , Keith S. Wilson (University of York) , Gideon J. Davies (University of York)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 71 , PAGES 114 - 120

State: Published (Approved)
Published: January 2015
Diamond Proposal Number(s): 1221

Abstract: The enzymatic degradation of plant cell-wall cellulose is central to many industrial processes, including second-generation biofuel production. Key players in this deconstruction are the fungal cellobiohydrolases (CBHs), notably those from family GH7 of the carbohydrate-active enzymes (CAZY) database, which are generally known as CBHI enzymes. Here, threedimensional structures are reported of the Aspergillus fumigatus CBHI Cel7A solved in uncomplexed and disaccharide-bound forms at resolutions of 1.8 and 1.5 A˚ , respectively. The product complex with a disaccharide in the +1 and +2 subsites adds to the growing three-dimensional insight into this family of industrially relevant biocatalysts.

Journal Keywords: cellulase; biofuels; carbohydrate-active enzyme; thermal stability

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I02-Macromolecular Crystallography

Added On: 27/03/2015 10:41

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