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Title 

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

Authors 

Seong Tae JeongHyung Kwoun KimSeung Jun KimSeung Wook ChiJae Gu PanTae Kwang OhSeong Eon Ryu

Publisher 

American Society for Biochemistry and Molecular Biology

Issue Date 

2002

Citation 

Journal of Biological Chemistry, vol. 277, no. 19, pp. 17041-17047

Keywords 

activation analysisbacteriacrystal structurefatty acidsbacterial enzymel1 lipasetriacylglycerol lipaseunclassified druganimal cellbinding site

Abstract 

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.

ISSN 

0021-9258

Link 

http://dx.doi.org/10.1074/jbc.M200640200

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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