Open AccessOverexpression, crystallization and preliminary X‐ray crystallographic analysis of β‐ N ‐acetylglucosaminidase from Thermotoga maritima encoded by the Tm0809 gene
Author(s) -
Lee Hyung Ho,
Jung Sang Taek
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112049020
Subject(s) - thermotoga maritima , crystallization , crystallography , monoclinic crystal system , ammonium sulfate , escherichia coli , chitin , gene , chemistry , domain (mathematical analysis) , crystal structure , stereochemistry , biology , biochemistry , organic chemistry , chromatography , chitosan , mathematical analysis , mathematics
β‐ N ‐acetylglucosaminidase (NagA) protein hs a chitin‐degrading activity and chitin is one of the most abundant polymers in nature. NagA contains a family 3 glycoside (GH3)‐type N‐terminal domain and a unique C‐terminal domain. The structurally uncharacterized C‐terminal domain of NagA may be involved in substrate specificity. To provide a structural basis for the substrate specificity of NagA, structural analysis of NagA from Thermotoga maritima encoded by the Tm0809 gene was initiated. NagA from T. maritima has been overexpressed in Escherichia coli and crystallized at 296 K using ammonium sulfate as a precipitant. Crystals of T. maritima NagA diffracted to 3.80 Å resolution and belonged to the monoclinic space group C 2, with unit‐cell parameters a = 231.15, b = 133.62, c = 140.88 Å, β = 89.97°. The crystallization of selenomethionyl‐substituted protein is in progress to solve the crystal structure of T. maritima NagA.