1KU0
Structure of the Bacillus stearothermophilus L1 lipase
Summary for 1KU0
Entry DOI | 10.2210/pdb1ku0/pdb |
Descriptor | L1 lipase, ZINC ION, CALCIUM ION, ... (4 entities in total) |
Functional Keywords | hydrolase, lipase |
Biological source | Geobacillus stearothermophilus |
Total number of polymer chains | 2 |
Total formula weight | 86595.26 |
Authors | Jeong, S.-T.,Kim, H.-K.,Kim, S.-J.,Chi, S.-W.,Pan, J.-G.,Oh, T.-K.,Ryu, S.-E. (deposition date: 2002-01-18, release date: 2002-08-21, Last modification date: 2024-03-13) |
Primary citation | 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 Cited by 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: 11859083DOI: 10.1074/jbc.M200640200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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