Crystal structure and functional characterization of a cold-active acetyl xylan esterase (PbAcE) from psychrophilic soil microbe Paenibacillus sp.open access
- Authors
- Park, Sun-Ha; Yoo, Wanki; Lee, Chang Woo; Jeong, Chang Sook; Shin, Seung Chul; Kim, Han-Woo; Park, Hyun; Kim, Kyeong Kyu; Kim, T. Doohun; Lee, Jun Hyuck
- Issue Date
- Oct-2018
- Publisher
- PUBLIC LIBRARY SCIENCE
- Citation
- PLOS ONE, v.13, no.10
- Journal Title
- PLOS ONE
- Volume
- 13
- Number
- 10
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/4242
- DOI
- 10.1371/journal.pone.0206260
- ISSN
- 1932-6203
- 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 hydrolyzes glucose penta-acetate and xylan acetate, reversibly producing acetyl xylan from xylan, and it shows higher activity at 4 degrees C than at 25 degrees 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 beta 4-alpha 3 and beta 5-alpha 4 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.
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