4GW3
Crystal Structure of the Lipase from Proteus mirabilis
Summary for 4GW3
| Entry DOI | 10.2210/pdb4gw3/pdb |
| Related | 4GXN |
| Descriptor | Putative lipase, CALCIUM ION, ISOPROPYL ALCOHOL, ... (6 entities in total) |
| Functional Keywords | lipase, hydrolase |
| Biological source | Proteus mirabilis |
| Total number of polymer chains | 1 |
| Total formula weight | 34559.90 |
| Authors | Korman, T.P. (deposition date: 2012-08-31, release date: 2013-02-06, Last modification date: 2024-02-28) |
| 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 Cited by 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: 23300806DOI: 10.1371/journal.pone.0052890 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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