4gxn

Diethylphosphonate Inhibited Structure of the Proteus mirabilis Lipase

spinqualitylabelsall models 4gxn, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4gxn is a 1 chain structure with sequence from Proteus mirabilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, DEP, PGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B4EVM3_PROMH 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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