4GXN

Diethylphosphonate Inhibited Structure of the Proteus mirabilis Lipase

Summary for 4GXN

• Entry DOI: 10.2210/pdb4gxn/pdb
• Related: 4GW3
• Descriptor: Putative lipase, CALCIUM ION, DIETHYL PHOSPHONATE, ... (5 entities in total)
• Functional Keywords: lipase, hydrolase, a/b hydrolase fold, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Proteus mirabilis
• Total number of polymer chains: 1
• Total formula weight: 34179.35

Authors

Korman, T.P.,Bowie, J.U. (deposition date: 2012-09-04, release date: 2013-02-06, Last modification date: 2024-10-16)

Primary citation

Korman, T.P.,Bowie, J.U.
Crystal Structure of Proteus mirabilis Lipase, a Novel Lipase from the Proteus/Psychrophilic Subfamily of Lipase Family I.1.
Plos One, 7:e52890-e52890, 2012

PubMed 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.

PubMed: 23300806
DOI: 10.1371/journal.pone.0052890

Experimental method

X-RAY DIFFRACTION (2.2 Å)