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Identification, Characterization, and Preliminary X-ray Diffraction Analysis of a Novel Esterase (ScEst) from Staphylococcus chromogenes

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Title
Identification, Characterization, and Preliminary X-ray Diffraction Analysis of a Novel Esterase (ScEst) from Staphylococcus chromogenes
Other Titles
병원성 미생물 (Staphylococcus chromogenes)유래 신규 에스터레이즈 효소의 서열 및 결정화 연구
Authors
Hwang, Jisub
전상근
이민주
유완기
장주원
김경규
Lee, Jun Hyuck
Do, Hackwon
김두헌
Keywords
Staphylococcus chromogenesX-ray crystallographycarboxylesterase
Issue Date
2022
Citation
Hwang, Jisub, et al. 2022. "Identification, Characterization, and Preliminary X-ray Diffraction Analysis of a Novel Esterase (ScEst) from Staphylococcus chromogenes". CRYSTALS, 12(4): 546-554.
Abstract
Ester prodrugs can develop novel antibiotics and have potential therapeutic applications against multiple drug-resistant bacteria. The antimicrobial activity of these prodrugs is activated after being cleaved by the esterases produced by the pathogen. Here, novel esterase ScEst originating from Staphylococcus chromogenes NCTC10530, which causes dairy cow mastitis, was identified, characterized, and analyzed using X-ray crystallography. The gene encoding ScEst was cloned into the pVFT1S vector and overexpressed in E. coli. The recombinant ScEst protein was obtained by affinity and size-exclusion purification. ScEst showed substrate preference for the short chain length of acyl derivatives. It was crystallized in an optimized solution composed of 0.25 M am-monium citrate tribasic (pH 7.0) and 20% PEG 3350 at 296 K. A total of 360 X-ray diffraction im-ages were collected at a 1.66 A resolution. ScEst crystal belongs to the space group of P212121 with the unit cell parameters of a = 50.23 A, b = 68.69 A, c = 71.15 A, and α = β = γ = 90°. Structure refinement after molecular replacement is under progress. Further biochemical studies will elu-cidate the hydrolysis mechanism of ScEst. Overall, this study is the first to report the functional characterization of an esterase from Staphylococcus chromogenes, which is potentially useful in elaborating its hydrolysis mechanism.
URI
https://repository.kopri.re.kr/handle/201206/13462
DOI
http://dx.doi.org/10.3390/cryst12040546
Type
Article
Station
해당사항없음
Indexed
SCIE
Appears in Collections  
2022-2022, Development of potential antibiotic compounds using polar organism resources (22-22) / Lee, Jun Hyuck (PM22030)
2022-2022, Development of microbial enzymes degrading recalcitrant materials from the Arctic Circle (22-22) / Kim, Han-Woo (PN22014)
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