KOPRI Repository

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

Cited 14 time in wos
Cited 17 time in scopus

Full metadata record

DC Field Value Language
dc.contributor.authorPark, Sun-Ha-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorKim, T. Doohun-
dc.contributor.authorKim, Kyeong Kyu-
dc.contributor.authorPark, Hyun-
dc.contributor.authorKim, Han-Woo-
dc.contributor.authorShin, Seung Chul-
dc.contributor.authorJeong, Chang Sook-
dc.contributor.authorLee, Chang Woo-
dc.contributor.authorYoo, Wanki-
dc.date.accessioned2019-08-23T05:30:06Z-
dc.date.available2019-08-23T05:30:06Z-
dc.date.issued2018-10-
dc.identifier.issn1932-6203-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/9664-
dc.description.abstractCold-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.en_US
dc.languageEnglish-
dc.language.isoen_USen_US
dc.subjectScience & Technology - Other Topicsen_US
dc.subject.classificationDasan Stationen_US
dc.titleCrystal structure and functional characterization of a cold-active acetyl xylan esterase (PbAcE) from psychrophilic soil microbe Paenibacillus sp.en_US
dc.title.alternative알라스카 동토 미생물 유래 저온성 acetyl xylan esterase (PbAcE) 효소의 구조 및 기능 연구en_US
dc.typeArticleen_US
dc.identifier.bibliographicCitationPark, Sun-Ha, et al. 2018. "Crystal structure and functional characterization of a cold-active acetyl xylan esterase (PbAcE) from psychrophilic soil microbe Paenibacillus sp.". <em>PLOS ONE</em>, 13(10): 1-18.-
dc.citation.titlePLOS ONEen_US
dc.citation.volume13en_US
dc.citation.number10en_US
dc.identifier.doi10.1371/journal.pone.0206260-
dc.citation.startPage1en_US
dc.citation.endPage18en_US
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2016:23.4375en_US
dc.subject.keywordAcetyl esteraseen_US
dc.subject.keywordCold-active enzymeen_US
dc.subject.keywordCrystal structureen_US
dc.subject.keywordPaenibacillus sp.en_US
dc.subject.keywordX-ray crystallographyen_US
dc.identifier.localId2018-0172-
dc.identifier.scopusid2-s2.0-85055832304-
dc.identifier.wosid000448823700098-
Appears in Collections  
2018-2018, Development of potential candidates as antibiotics based on polar genetic resources (18-18) / Lee, Jun Hyuck (PE18210)
2018-2018, Application study on the Arctic cold-active enzyme degrading organic carbon compounds (18-18) / Kim, Han-Woo (PN18082)
2017-2018, Application study on the Arctic cold-active enzyme degrading organic carbon compounds (17-18) / Lee, Jun Hyuck; Kim, Han-Woo (PN17083; PN18082)
Files in This Item

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse