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Crystal structure and functional characterization of a cold-active acetyl xylan esterase (PbAcE) from psychrophilic soil microbe Paenibacillus sp.

Cited 2 time in wos
Cited 2 time in scopus
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Title
Crystal structure and functional characterization of a cold-active acetyl xylan esterase (PbAcE) from psychrophilic soil microbe Paenibacillus sp.
Other Titles
알라스카 동토 미생물 유래 저온성 acetyl xylan esterase (PbAcE) 효소의 구조 및 기능 연구
Authors
Park, Sun-Ha
Lee, Jun Hyuck
Kim, T. Doohun
Kim, Kyeong Kyu
Park, Hyun
Kim, Han-Woo
Shin, Seung Chul
Jeong, Chang Sook
Lee, Chang Woo
Yoo, Wanki
Subject
Science & Technology - Other Topics
Keywords
Acetyl esterase; Cold-active enzyme; Crystal structure; Paenibacillus sp.; X-ray crystallography
Issue Date
2018-10
Citation
Park, Sun-Ha, et al. 2018. "Crystal structure and functional characterization of a cold-active acetyl xylan esterase (PbAcE) from psychrophilic soil microbe Paenibacillus sp.". PLOS ONE, 13(10): 1-18.
Abstract
Cold-active acetyl xylan esterases allow for reduced bioreactor heating costs in bioenergy production. Here, we isolated and characterized a cold-active acetyl xylan esterase (PbAcE) from the psychrophilic soil microbe Paenibacillus sp. R4. The enzyme reversibly hydrolyzes glucose penta-acetate and xylan acetate, alternatively producing acetyl xylan from xylan, and it shows higher activity at 4°C than at 25°C. We solved the crystal structure of PbAcE at 2.1-A resolution to investigate its active site and the reason for its low-temperature activity. Structural analysis showed that PbAcE forms a hexamer with a central substrate binding tunnel, and the inter-subunit interactions are relatively weak compared with those of its mesophilic and thermophilic homologs. PbAcE also has a shorter loop and different residue composition in the β4?α3 and β5?α4 regions near the substrate binding site. Flexible subunit movements and different active site loop conformations may enable the strong low-temperature activity and broad substrate specificity of PbAcE. In addition, PbAcE was found to have strong activity against antibiotic compound substrates, such as cefotaxime and 7-amino cephalosporanic acid (7-ACA). In conclusion, the PbAcE structure and our biochemical results provide the first example of a cold-active acetyl xylan esterase and a starting template for structure-based protein engineering.
URI
http://repository.kopri.re.kr/handle/201206/9664
DOI
http://dx.doi.org/10.1371/journal.pone.0206260
ISSN
1932-6203
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