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

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dc.contributor.authorPark, Sun-Ha-
dc.contributor.authorLee, Chang Woo-
dc.contributor.authorJeong, Chang-Sook-
dc.contributor.authorLee, Jun Hyuck-
dc.date.accessioned2021-07-22T06:28:48Z-
dc.date.available2021-07-22T06:28:48Z-
dc.date.issued2019-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/12292-
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 hydrolyzes glucose penta-acetate and xylan acetate, reversibly 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.languageEnglishen_US
dc.language.isoenen_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 cetyl xylan esterase (PbAcE) 효소의 구조와 기능 연구en_US
dc.typePosteren_US
dc.identifier.bibliographicCitationPark, Sun-Ha, et al. 2019. Crystal structure and functional characterization of a cold-active acetyl xylan esterase (PbAcE) from psychrophilic soil microbe Paenibacillus sp.. 2019 Federation of the Korean Societies for Biomolecular Sciences (FKSBS) Conference. Ewha Womans University. 2019.01.10~2019.01.12.en_US
dc.citation.conferenceDate2019.01.10~2019.01.12en_US
dc.citation.conferenceName2019 Federation of the Korean Societies for Biomolecular Sciences (FKSBS) Conferenceen_US
dc.citation.conferencePlaceEwha Womans Universityen_US
dc.description.articleClassification포스터-
dc.identifier.localId2019-0266-
Appears in Collections  
2019-2019, Development of potential candidates as antibiotics based on polar genetic resources (19-19) / Lee, Jun Hyuck (PE19210)
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