Crystallization and preliminary X-ray analyses of the active and the inactive forms of family GH-8 chitosanase with subclass II specificity from Bacillus sp. strain K17.
Chitosanase from Bacillus sp. strain K17 (ChoK) belongs to glycoside hydrolase family 8 and exhibits subclass II specificity. The purified protein is structurally stable over a wide pH range (3-10), but is active in a much narrower pH range (4.5-7.5), with optimal activity around pH 6.0. The protein has been successfully crystallized at two different pH values corresponding to the active and inactive states. The crystals diffract to 1.5 and 2.0 A resolution, respectively.
Sakihama
Yuri
Y
Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259-B4 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.
Adachi
Wataru
W
Shimizu
Shinji
S
Sunami
Tomoko
T
Fukazawa
Tetsuya
T
Suzuki
Mamie
M
Yatsunami
Rie
R
Nakamura
Satoshi
S
Takénaka
Akio
A
D001407:Bacillus / Q000145:classification / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004789:Enzyme Activation; D004795:Enzyme Stability; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration
D006026:Glycoside Hydrolases; C019868:chitosanase