Open AccessHeterologous expression, crystallization and preliminary X‐ray characterization of CcCel6C, a glycoside hydrolase family 6 enzyme from the basidiomycete Coprinopsis cinerea
Author(s) -
Kurakata Yuma,
Tonozuka Takashi,
Liu Yuan,
Kaneko Satoshi,
Nishikawa Atsushi,
Fukuda Kiyoharu,
Yoshida Makoto
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910804284x
Subject(s) - glycoside hydrolase , heterologous expression , enzyme , biology , escherichia coli , hydrolase , gene , biochemistry , cellulase , triclinic crystal system , stereochemistry , chemistry , microbiology and biotechnology , genetics , recombinant dna , crystal structure , crystallography
CcCel6C is a gene that encodes a glycoside hydrolase family 6 (GH6) enzyme in the Coprinopsis cinerea genome. In the evolutionary tree of GH6 enzymes, the encoded enzyme was closely related to Cel6B from Humicola insolens , previously called endoglucanase VI, while its amino‐acid sequence revealed a region corresponding to the C‐terminal active‐site‐enclosing loop typical of cellobiohydrolase II. Here, the crystallization of CcCel6C produced in Escherichia coli is reported. The square prismatic crystal belonged to the triclinic space group P 1, with unit‐cell parameters a = 44.04, b = 45.11, c = 48.90 Å, α = 77.81, β = 87.34, γ = 68.79°. Diffraction data were collected to 1.6 Å resolution.