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Structural insight into industrially relevant glucoamylases: flexible positions of starch-binding domains

DOI: 10.1107/S2059798318004989 DOI Help

Authors: Christian Roth (University of York) , Olga V. Moroz (University of York) , Antonio Ariza (University of York) , Lars K. Skov (Novozymes A/S) , Keiichi Ayabe (Novozymes Japan Ltd) , Gideon J. Davies (University of York) , Keith S. Wilson (University of York)
Co-authored by industrial partner: Yes

Type: Journal Paper
Journal: Acta Crystallographica Section D Structural Biology , VOL 74 , PAGES 463 - 470

State: Published (Approved)
Published: May 2018
Diamond Proposal Number(s): 1221

Abstract: Glucoamylases are one of the most important classes of enzymes in the industrial degradation of starch biomass. They consist of a catalytic domain and a carbohydrate-binding domain (CBM), with the latter being important for the interaction with the polymeric substrate. Whereas the catalytic mechanisms and structures of the individual domains are well known, the spatial arrangement of the domains with respect to each other and its influence on activity are not fully understood. Here, the structures of three industrially used fungal glucoamylases, two of which are full length, have been crystallized and determined. It is shown for the first time that the relative orientation between the CBM and the catalytic domain is flexible, as they can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The flexibility in the orientations of the two domains presented a considerable challenge for the crystallization of the enzymes.

Journal Keywords: starch biomass degradation; glucoamylases; carbohydrate-binding module; Penicillium oxalicum; Hormoconis resinae; Aspergillus niger

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Other Facilities: ESRF