Structural highlights
Publication Abstract from PubMed
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.
Crystal Structure of Proteus mirabilis Lipase, a Novel Lipase from the Proteus/Psychrophilic Subfamily of Lipase Family I.1.,Korman TP, Bowie JU PLoS One. 2012;7(12):e52890. doi: 10.1371/journal.pone.0052890. Epub 2012 Dec 26. PMID:23300806[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Korman TP, Bowie JU. Crystal Structure of Proteus mirabilis Lipase, a Novel Lipase from the Proteus/Psychrophilic Subfamily of Lipase Family I.1. PLoS One. 2012;7(12):e52890. doi: 10.1371/journal.pone.0052890. Epub 2012 Dec 26. PMID:23300806 doi:http://dx.doi.org/10.1371/journal.pone.0052890
