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Structure of the GH9 glucosidase/glucosaminidase from Vibrio cholerae

DOI: 10.1107/S2053230X18011019 DOI Help

Authors: Liang Wu (The 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 74 , PAGES 512 - 523

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

Open Access Open Access

Abstract: Glycoside hydrolase family 9 (GH9) of carbohydrate-processing enzymes primarily consists of inverting endoglucanases. A subgroup of GH9 enzymes are believed to act as exo-glucosidases or exo-glucosaminidases, with many being found in organisms of the family Vibrionaceae, where they are proposed to function within the chitin-catabolism pathway. Here, it is shown that the GH9 enzyme from the pathogen Vibrio cholerae (hereafter referred to as VC0615) is active on both chitosan-derived and β-glucoside substrates. The structure of VC0615 at 3.17 Å resolution is reported from a crystal form with poor diffraction and lattice disorder. VC0615 was highly refractory to crystallization efforts, with crystals only appearing using a high protein concentration under conditions containing the precipitant poly-γ-glutamic acid (PGA). The structure is highly mobile within the crystal lattice, which is likely to reflect steric clashes between symmetry molecules which destabilize crystal packing. The overall tertiary structure of VC0615 is well resolved even at 3.17 Å resolution, which has allowed the structural basis for the exo-glucosidase/glucosaminidase activity of this enzyme to be investigated.

Journal Keywords: glycoside hydrolase; enzymes; carbohydrates; VC0615; glucosidase; glucosaminidases; Vibrio; hydrolases

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography


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