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Title: Crystallization and Preliminary X-ray Diffraction Analysis of the Glucuronoyl Esterase Catalytic Domain from Hypocrea jecorina

Author
item WOOD, S - ARGONNE NATL LAB
item Li, Xin Liang
item Cotta, Michael
item BIELY, P - SLOVAK ACADEMY OF SCI
item DUKE, N - ARGONNE NATL LAB
item SCHIFFER, M - ARGONNE NATL LAB
item POKKULURI, P - ARGONNE NATL LAB

Submitted to: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 3/1/2008
Publication Date: 4/1/2008
Citation: Wood, S.J., Li, X., Cotta, M.A., Biely, P., Duke, N.E., Schiffer, M., Pokkuluri, P.R. 2008. Crystallization and Preliminary X-ray Diffraction Analysis of the Glucuronoyl Esterase Catalytic Domain from Hypocrea jecorina. Acta Crystallographica Section F. 64(4):255-257.

Interpretive Summary: Continued development of a carbohydrate-based system for production of fuels and chemicals to replace petroleum will require the recruitment of new renewable materials to add to the current corn starch based feedstocks. These materials will include agricultural residues like straws and stovers and new dedicated energy crops such as switchgrass and poplars. In all cases, the vast majority of carbohydrates in these candidate feedstocks are contained in plant cell walls. The major polymers of plant cell walls include cellulose, hemicellulose, and lignin which are intermeshed in a complex organization which provides structural integrity to the plant. The association of lignin with the hemicellulose (of which xylan is the most abundant type) has long been recognized as a likely limitation on the efficient conversion of cell wall polysaccharides to monomer sugars. Several types of linkages between lignin and xylan in plant cell walls have been described. In collaboration with Professor Peter Biely in Slovakia, we have identified the microbial genes coding for the enzymes that might be specifically responsible for breaking the bond between lignin and xylan (glucuronoyl esterase). This paper reports the successful crystallization of the enzyme through collaboration between the Argonne National Laboratory and the National Center for Agricultural Utilization Research. Crystallization of the enzyme is a critical step for the determination of its structure. The results reported will help us to understand the role of this type of enzyme in plant cell wall biodegradation and efficient bioconversion of cellulosic biomass into biofuels and bioproducts.

Technical Abstract: The catalytic domain of the glucuronoyl esterase from Hypocrea jecorina (anamorph Trichoderma reesei) was over-expressed, purified, and crystallized by sitting-drop vapor-diffusion method using 1.4 M sodium/potassium phosphate pH 6.9. Crystals had space group P212121 and X-ray diffraction data were collected to 1.9 Å resolution. This is the first enzyme with glucoronyl esterase activity to be crystallized; its structure will be valuable in lignocellulose degradation research.