5B5S

Crystal structure of a carbohydrate esterase family 3 from Talaromyces cellulolyticus

Replaces:  3X0H

Summary for 5B5S

• Entry DOI: 10.2210/pdb5b5s/pdb
• Descriptor: Acetic acid, octyl beta-D-glucopyranoside, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: biomass, carbohydrate esterase, catalytic triad, disulfide bond, saccharification xylanase, hydrolase
• Biological source: Talaromyces cellulolyticus
• Total number of polymer chains: 1
• Total formula weight: 23118.12

Authors

Watanabe, M.,Ishikawa, K. (deposition date: 2016-05-16, release date: 2016-11-16, Last modification date: 2024-10-30)

Primary citation

Watanabe, M.,Fukada, H.,Inoue, H.,Ishikawa, K.
Crystal structure of an acetylesterase from Talaromyces cellulolyticus and the importance of a disulfide bond near the active site
Febs Lett., 589:1200-1206, 2015

PubMed Abstract: Carbohydrate esterase catalyzes the de-O or de-N-acylation of substituted saccharides in plant cell walls and thus has great potential for industrial biomass saccharification. We recently identified the putative carbohydrate esterase family 3 (CE3) from Talaromyces cellulolyticus. Here, we prepared the recombinant catalytic domain of the enzyme and crystallized it. The crystal structure was determined to 1.5 Å resolution. From the structural analysis, it was elucidated that a n-octyl-β-D-glucopyranoside bound to near the catalytic triad (Ser10, Asp179 and His182) and was buried in the active site cavity. Site-directed mutagenesis showed that the N-terminal disulfide bond located near the catalytic triad is involved in the activity and structural stability of the enzyme.

PubMed: 25825334
DOI: 10.1016/j.febslet.2015.03.020

Experimental method

X-RAY DIFFRACTION (1.5 Å)