In:
Acta Crystallographica Section F Structural Biology Communications, International Union of Crystallography (IUCr), Vol. 71, No. 4 ( 2015-04-01), p. 427-433
Abstract:
Vibrio harveyi β- N -acetylglucosaminidase ( Vh GlcNAcase) is a new member of the GH20 glycoside hydrolase family responsible for the complete degradation of chitin fragments, with N -acetylglucosamine (GlcNAc) monomers as the final products. In this study, the crystallization and preliminary crystallographic data of wild-type Vh GlcNAcase and its catalytically inactive mutant D437A in the absence and the presence of substrate are reported. Crystals of wild-type Vh GlcNAcase were grown in 0.1 M sodium acetate pH 4.6, 1.4 M sodium malonate, while crystals of the D437A mutant were obtained in 0.1 M bis-tris pH 7.5, 0.1 M sodium acetate, 20% PEG 3350. X-ray data from the wild-type and the mutant crystals were collected at a synchrotron-radiation light source and were complete to a resolution of 2.5 Å. All crystals were composed of the same type of dimer, with the substrate N , N ′-diacetylglucosamine (GlcNAc 2 or diNAG) used for soaking was cleaved by the active enzyme, leaving only a single GlcNAc molecule bound to the protein.
Type of Medium:
Online Resource
ISSN:
2053-230X
DOI:
10.1107/S2053230X1500415X
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2015
detail.hit.zdb_id:
2175956-X
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