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Communication

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

1
Department of Chemistry, College of Natural Science, Sookmyung Women’s University, Seoul 04310, Korea
2
Unit of Research for Practical Application, Korea Polar Research Institute, Incheon 21990, Korea
3
Department of Polar Sciences, University of Science and Technology, Incheon 21990, Korea
4
Department of Precision Medicine, School of Medicine, Sungkyunkwan University, Suwon 16419, Korea
*
Authors to whom correspondence should be addressed.
These two authors contributed equally to this work.
Crystals 2020, 10(11), 963; https://doi.org/10.3390/cryst10110963
Received: 25 September 2020 / Revised: 21 October 2020 / Accepted: 22 October 2020 / Published: 23 October 2020
Hormone sensitive lipase is a central enzyme in triacylglycerol hydrolysis, lipid modification, and transformation 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 Å with an Rmerge of 7.3%. The crystals of HaLip1 belong to the P212121, with unit cell parameters of a = 54.6 Å, b = 59.5 Å, and c = 82.9 Å. View Full-Text
Keywords: hormone sensitive lipase; psychrophilic bacterium; crystallization hormone sensitive lipase; psychrophilic bacterium; crystallization
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MDPI and ACS Style

Jeon, S.; Hwang, J.; Yoo, W.; Do, H.; Kim, H.-W.; Kim, K.K.; Lee, J.H.; Kim, T.D. Crystallization and Preliminary X-ray Diffraction Study of a Novel Bacterial Homologue of Mammalian Hormone-Sensitive Lipase (halip1) from Halocynthiibacter arcticus. Crystals 2020, 10, 963. https://doi.org/10.3390/cryst10110963

AMA Style

Jeon S, Hwang J, Yoo W, Do H, Kim H-W, Kim KK, Lee JH, Kim TD. Crystallization and Preliminary X-ray Diffraction Study of a Novel Bacterial Homologue of Mammalian Hormone-Sensitive Lipase (halip1) from Halocynthiibacter arcticus. Crystals. 2020; 10(11):963. https://doi.org/10.3390/cryst10110963

Chicago/Turabian Style

Jeon, Sangeun, Jisub Hwang, Wanki Yoo, Hackwon Do, Han-Woo Kim, Kyeong K. Kim, Jun H. Lee, and T. D. Kim. 2020. "Crystallization and Preliminary X-ray Diffraction Study of a Novel Bacterial Homologue of Mammalian Hormone-Sensitive Lipase (halip1) from Halocynthiibacter arcticus" Crystals 10, no. 11: 963. https://doi.org/10.3390/cryst10110963

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