Crystal Structure of Proteus mirabilis Lipase,a Novel Lipase from the Proteus/Psychrophilic Subfamily of Lipase Family I.1 |
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| Authors: | Tyler P Korman James U Bowie |
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| Institution: | 1. Department of Chemistry and Biochemisty, University of California Los Angeles, Los Angeles, California, United States of America.; 2. UCLA-DOE Institute of Genomics and Proteomics, University of California Los Angeles, Los Angeles, California, United States of America.; 3. Molecular Biology Institute, University of California Los Angeles, Los Angeles, California, United States of America.; Monash University, Australia, |
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| Abstract: | Bacterial lipases from family I.1 and I.2 catalyze the hydrolysis of triacylglycerol between 25–45°C and are used extensively as biocatalysts. The lipase from Proteus mirabilis belongs to the Proteus/psychrophilic subfamily of lipase family I.1 and is a promising catalyst for biodiesel production because it can tolerate high amounts of water in the reaction. Here we present the crystal structure of the Proteus mirabilis lipase, a member of the Proteus/psychrophilic subfamily of I.1lipases. The structure of the Proteus mirabilis lipase was solved in the absence and presence of a bound phosphonate inhibitor. Unexpectedly, both the apo and inhibitor bound forms of P. mirabilis lipase were found to be in a closed conformation. The structure reveals a unique oxyanion hole and a wide active site that is solvent accessible even in the closed conformation. A distinct mechanism for Ca2+ coordination may explain how these lipases can fold without specific chaperones. |
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