1KU0

Structure of the Bacillus stearothermophilus L1 lipase

1KU0 の概要

• エントリーDOI: 10.2210/pdb1ku0/pdb
• 分子名称: L1 lipase, ZINC ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, lipase
• 由来する生物種: Geobacillus stearothermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 86595.26

構造登録者

Jeong, S.-T.,Kim, H.-K.,Kim, S.-J.,Chi, S.-W.,Pan, J.-G.,Oh, T.-K.,Ryu, S.-E. (登録日: 2002-01-18, 公開日: 2002-08-21, 最終更新日: 2024-03-13)

主引用文献

Jeong, S.T.,Kim, H.K.,Kim, S.J.,Chi, S.W.,Pan, J.G.,Oh, T.K.,Ryu, S.E.
Novel zinc-binding center and a temperature switch in the Bacillus stearothermophilus L1 lipase.
J.Biol.Chem., 277:17041-17047, 2002

PubMed 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 I.5. We report here the first crystal structure of the lipase family I.5, the structure of a thermoalkalophilic lipase from Bacillus stearothermophilus L1 (L1 lipase) determined at 2.0-A 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 I.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 I.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.

PubMed: 11859083
DOI: 10.1074/jbc.M200640200

実験手法

X-RAY DIFFRACTION (2 Å)