Crystallization and preliminary X-ray crystallographic analysis of BxlA, an intracellular beta-D-xylosidase from Streptomyces thermoviolaceus OPC-520.
BxlA from Streptomyces thermoviolaceus OPC-520, together with the extracellular BxlE and the integral membrane proteins BxlF and BxlG, constitutes a xylanolytic system that participates in the intracellular transport of xylan-degradation products and the production of xylose. To elucidate the mechanism of the hydrolytic degradation of xylooligosaccharides to xylose at the atomic level, X-ray structural analysis of BxlA was attempted. The recombinant BxlA protein (molecular weight 82 kDa) was crystallized by the hanging-drop vapour-diffusion method at 289 K. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 142.2, b = 129.5, c = 101.4 A, beta = 119.8 degrees , and contained two molecules per asymmetric unit (V(M) = 2.47 A(3) Da(-1)). Diffraction data were collected to a resolution to 2.50 A and provided a data set with an overall R(merge) of 8.3%.
Morioka
Hideaki
H
Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences, Takatsuki, Osaka 569-1094, Japan.
Miki
Yasuhiro
Y
Saito
Kei
K
Tomoo
Koji
K
Ishida
Toshimasa
T
Hasegawa
Tomokazu
T
Yamano
Akihito
A
Takada
Chiaki
C
Miyamoto
Katsushiro
K
Tsujibo
Hiroshi
H
D003460:Crystallization; D018360:Crystallography, X-Ray; D013302:Streptomyces / Q000201:enzymology*; D014995:Xylosidases / Q000737:chemistry*
D014995:Xylosidases; C026579:exo-1,4-beta-D-xylosidase