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Crystallization and Preliminary X-ray Diffraction Study of a Novel Bacterial Homologue of Mammalian Hormone-Sensitive Lipase (halip1) from Halocynthiibacter arcticus

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Title
Crystallization and Preliminary X-ray Diffraction Study of a Novel Bacterial Homologue of Mammalian Hormone-Sensitive Lipase (halip1) from Halocynthiibacter arcticus
Other Titles
북극 해양 퇴적물에서 분리된 Halocynthiibacter Arcticus 균주 유래 저온성 Lipase (halip1) 효소의 결정화와 구조분석을 위한 X-선 회절연구
Authors
Jeon, Sangeun
Hwang, Jisub
Yoo, Wanki
Do, Hackwon
Kim, Han-Woo
Kim, Kyeong Kyu
Lee, Jun Hyuck
Kim, T. Doohun
Subject
Crystallography; Materials Science
Keywords
hormone sensitive lipase; psychrophilic bacterium; crystallization
Issue Date
2020-11
Citation
Jeon, Sangeun, et al. 2020. "Crystallization and Preliminary X-ray Diffraction Study of a Novel Bacterial Homologue of Mammalian Hormone-Sensitive Lipase (halip1) from Halocynthiibacter arcticus". CRYSTALS, 10(11): 963-969.
Abstract
Hormone sensitive lipase is a central enzyme in triacylglycerol hydrolysis, lipid modification, and transformaton of various lipids. Microbial hormone-sensitive lipases, which are highly similar to a catalytic domain of mammalian equivalents, have attracted strong attention due to their application potentials. Here, characterization and a preliminary X-ray crystallographic analysis of a novel bacterial homologue of hormone-sensitive lipase (HaLip1) from Halocynthiibacter arcticus is reported. Sequence analysis shows that HaLip1 has a conserved serine residue within the GDSAG motif. In addition, a characteristic HGGG motif for oxyanion formation was identified. The HaLip1 protein was overexpressed in E. coli. SDS-PAGE, overlay assay, and mass analysis were performed to confirm purity and activity of HaLip1 protein. Furthermore, HaLip1 was crystallized in a condtion consisting of 25 % (w/v) PEG 3350, 0.1 M Hepes-KOH, pH 7.5, 0.2 M sodium chloride. Diffraction data were processed to 1.30 A with Rmerge of 7.3%. The crystals of HaLip1 belong to the P212121, with unit cell parameters of a = 54.6 A, b = 59.5 A, and c = 82.9 A.
URI
https://repository.kopri.re.kr/handle/201206/11850
DOI
http://dx.doi.org/10.3390/cryst10110963
Appears in Collections  
2020-2020, Development of potential candidates as antibiotics based on polar genetic resources (20-20) / Lee, Jun Hyuck (PM20030)
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