Crystal structure and functional characterization of a cold-active acetyl xylan esterase (PbAcE) from psychrophilic soil microbe Paenibacillus sp.
DC Field | Value | Language |
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dc.contributor.author | Park, Sun-Ha | - |
dc.contributor.author | Yoo, Wanki | - |
dc.contributor.author | Lee, Chang Woo | - |
dc.contributor.author | Jeong, Chang Sook | - |
dc.contributor.author | Shin, Seung Chul | - |
dc.contributor.author | Kim, Han-Woo | - |
dc.contributor.author | Park, Hyun | - |
dc.contributor.author | Kim, Kyeong Kyu | - |
dc.contributor.author | Kim, T. Doohun | - |
dc.contributor.author | Lee, Jun Hyuck | - |
dc.date.available | 2021-02-22T08:45:35Z | - |
dc.date.issued | 2018-10 | - |
dc.identifier.issn | 1932-6203 | - |
dc.identifier.uri | https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/4242 | - |
dc.description.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. | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | PUBLIC LIBRARY SCIENCE | - |
dc.title | Crystal structure and functional characterization of a cold-active acetyl xylan esterase (PbAcE) from psychrophilic soil microbe Paenibacillus sp. | - |
dc.type | Article | - |
dc.publisher.location | 미국 | - |
dc.identifier.doi | 10.1371/journal.pone.0206260 | - |
dc.identifier.scopusid | 2-s2.0-85055832304 | - |
dc.identifier.wosid | 000448823700098 | - |
dc.identifier.bibliographicCitation | PLOS ONE, v.13, no.10 | - |
dc.citation.title | PLOS ONE | - |
dc.citation.volume | 13 | - |
dc.citation.number | 10 | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | Y | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.subject.keywordPlus | CEPHALOSPORIN-C | - |
dc.subject.keywordPlus | SUBSTRATE-SPECIFICITY | - |
dc.subject.keywordPlus | BACILLUS-SUBTILIS | - |
dc.subject.keywordPlus | ENZYME | - |
dc.subject.keywordPlus | FAMILY | - |
dc.subject.keywordPlus | HYDROLASE | - |
dc.identifier.url | https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0206260 | - |
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