Crystallization and preliminary X-ray diffraction analysis of the glucuronoyl esterase catalytic domain from Hypocrea jecorina.
The catalytic domain of the glucuronoyl esterase from Hypocrea jecorina (anamorph Trichoderma reesei) was overexpresssed, purified and crystallized by the sitting-drop vapor-diffusion method using 1.4 M sodium/potassium phosphate pH 6.9. The crystals belonged to space group P2(1)2(1)2(1) and X-ray diffraction data were collected to 1.9 A resolution. This is the first enzyme with glucoronoyl esterase activity to be crystallized; its structure will be valuable in lignocellulose-degradation research.
Wood
S J
SJ
Biosciences Division, Argonne National Laboratory, Argonne, IL 60439, USA.
Li
X-L
XL
Cotta
M A
MA
Biely
P
P
Duke
N E C
NE
Schiffer
M
M
Pokkuluri
P R
PR
D020134:Catalytic Domain / Q000235:genetics; D003460:Crystallization; D004950:Esterases / Q000737:chemistry* / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D005965:Glucuronates / Q000737:chemistry* / Q000378:metabolism; D035901:Hypocrea / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry; D013379:Substrate Specificity; D014242:Trichoderma / Q000201:enzymology; D014961:X-Ray Diffraction
D005656:Fungal Proteins; D005965:Glucuronates; D011994:Recombinant Proteins; D004950:Esterases