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Sequence Analysis and Preliminary X-ray Crystallographic Analysis of an Acetylesterase (LgEstI) from Lactococcus garvieae

Cited 1 time in wos
Cited 1 time in scopus

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dc.contributor.authorDo, Hackwon-
dc.contributor.authorWang, Ying-
dc.contributor.authorLee, Chang Woo-
dc.contributor.authorYoo, Wanki-
dc.contributor.authorJeon, Sangeun-
dc.contributor.authorHwang, Jisub-
dc.contributor.authorLee, Min Ju-
dc.contributor.authorKim, Kyeong Kyu-
dc.contributor.authorKim, Han-Woo-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorKim, T. Doohun-
dc.date.accessioned2022-07-29T04:58:18Z-
dc.date.available2022-07-29T04:58:18Z-
dc.date.issued2022-01-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/13714-
dc.description.abstractA gene encoding LgEstI was cloned from a bacterial fish pathogen, Lactococcus garvieae. Sequence and bioinformatic analysis revealed that LgEstI is close to the acetyl esterase family and had maximum similarity to a hydrolase (UniProt: Q5UQ83) from Acanthamoeba polyphaga mimivirus (APMV). Here, we present the results of LgEstI overexpression and purification, and its preliminary X-ray crystallographic analysis. The wild-type LgEstI protein was overexpressed in Escherichia coli, and its enzymatic activity was tested using p-nitrophenyl of varying lengths. LgEstI protein exhib-ited higher esterase activity toward p-nitrophenyl acetate. To better understand the mechanism un-derlying LgEstI activity and subject it to protein engineering, we determined the high-resolution crystal structure of LgEstI. First, the wild-type LgEstI protein was crystallized in 0.1 M Tris-HCl buffer (pH 7.1), 0.2 M calcium acetate hydrate, and 19% (w/v) PEG 3000, and the native X-ray dif-fraction dataset was collected up to 2.0 A resolution. The crystal structure was successfully deter-mined using a molecular replacement method, and structure refinement and model building are underway. The upcoming complete structural information of LgEstI may elucidate the substrate-binding mechanism and provide novel strategies for subjecting LgEstI to protein engineering.en_US
dc.languageEnglishen_US
dc.language.isoenen_US
dc.subjectCrystallographyen_US
dc.subjectMaterials Scienceen_US
dc.subject.classification해당사항없음en_US
dc.titleSequence Analysis and Preliminary X-ray Crystallographic Analysis of an Acetylesterase (LgEstI) from Lactococcus garvieaeen_US
dc.title.alternative해양어류 병원성 미생물 (Lactococcus garvieae)유래 아세틸에스터레이즈 효소의 서열 및 결정화 연구en_US
dc.typeArticleen_US
dc.identifier.bibliographicCitationDo, Hackwon, et al. 2022. "Sequence Analysis and Preliminary X-ray Crystallographic Analysis of an Acetylesterase (LgEstI) from Lactococcus garvieae". <em>CRYSTALS</em>, 12(1): 1-8.-
dc.citation.titleCRYSTALSen_US
dc.citation.volume12en_US
dc.citation.number1en_US
dc.identifier.doi10.3390/cryst12010046-
dc.citation.startPage1en_US
dc.citation.endPage8en_US
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2020:36en_US
dc.subject.keywordesteraseen_US
dc.subject.keywordLactococcus garvieaeen_US
dc.subject.keywordX-ray crystallographyen_US
dc.identifier.localId2022-0003-
dc.identifier.scopusid2-s2.0-85122192852-
dc.identifier.wosid000757989200001-
Appears in Collections  
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2021-2021, Development of microbial enzymes degrading recalcitrant materials from the Arctic Circle (21-21) / Kim, Han-Woo (PN21014)
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