Novel zinc-binding center and a temperature switch in the Bacillus stearothermophilus L1 lipase

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Novel zinc-binding center and a temperature switch in the Bacillus stearothermophilus L1 lipase
Seong Tae Jeong; Hyung Kwoun Kim; Seung Jun KimSeung Wook Chi; Jae Gu Pan; Tae Kwang Oh; Seong Eon Ryu
Bibliographic Citation
Journal of Biological Chemistry, vol. 277, no. 19, pp. 17041-17047
Publication Year
The bacterial thermoalkalophilic lipases optimally hydrolyze saturated fatty acids at elevated temperatures. They also have significant sequence homology with staphylococcal lipases, and both the thermoalkalophilic and staphylococcal lipases are grouped as the lipase family 1.5. We report here the first crystal structure of the lipase family 1.5, the structure of a thermoalkalophilic lipase from Bacillus stearothermophilus L1 (L1 lipase) determined at 2.0-? resolution. The structure is in a closed conformation, and the active site is buried under a long lid helix. Unexpectedly, the structure exhibits a zinc-binding site in an extra domain that accounts for the larger molecular size of the family 1.5 enzymes in comparison to other microbial lipases. The zinc-coordinated extra domain makes tight interactions with the loop extended from the C terminus of the lid helix, suggesting that the activation of the family 1.5 lipases may be regulated by the strength of the interactions. The unusually long lid helix makes strong hydrophobic interactions with its neighbors. The structural information together with previous biochemical observations indicate that the temperature-mediated lid opening is triggered by the thermal dissociation of the hydrophobic interactions.
Amer Soc Biochemistry Molecular Biology Inc
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Division of Biomedical Research > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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