Title : Crystal Structure of Proteus mirabilis Lipase, a Novel Lipase from the Proteus\/Psychrophilic Subfamily of Lipase Family I.1 - Korman_2012_PLoS.One_7_e52890 |
Author(s) : Korman TP , Bowie JU |
Ref : PLoS ONE , 7 :e52890 , 2012 |
Abstract :
Bacterial lipases from family I.1 and I.2 catalyze the hydrolysis of triacylglycerol between 25-45 degrees 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 Ca(2+) coordination may explain how these lipases can fold without specific chaperones. |
PubMedSearch : Korman_2012_PLoS.One_7_e52890 |
PubMedID: 23300806 |
Gene_locus related to this paper: promi-c2lfd0 |
Inhibitor | Diethyl-hydrogen-phosphate |
Substrate | Paraoxon |
Gene_locus | promi-c2lfd0 |
Family | Bacterial_lip_FamI.1 |
Structure | 4GXN 4GW3 |
Korman TP, Bowie JU (2012)
Crystal Structure of Proteus mirabilis Lipase, a Novel Lipase from the Proteus\/Psychrophilic Subfamily of Lipase Family I.1
PLoS ONE
7 :e52890
Korman TP, Bowie JU (2012)
PLoS ONE
7 :e52890