2zj6

Crystal structure of D337A mutant of Pseudomonas sp. MIS38 lipase

spinqualitylabelsall models 2zj6, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zj6 is a 1 chain structure with sequence from Pseudomonas sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, ZN Related: 2z8x, 2z8z, 2zj7 Activity: Triacylglycerol lipase, with EC number 3.1.1.3 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed A family I.3 lipase from Pseudomonas sp. MIS38 (PML) contains three Ca(2+)-binding sites (Ca1-Ca3) in the N-catalytic domain. Of them, the Ca1 site is formed only in an open conformation. To analyze the role of these Ca(2+)-binding sites, three mutant proteins D157A-PML, D275A-PML and D337A-PML, which are designed to remove the Ca1, Ca2 and Ca3 sites, respectively, were constructed. Of them, the crystal structures of D157A-PML and D337A-PML in a closed conformation were determined. Both structures are nearly identical to that of the wild-type protein, except that the Ca3 site is missing in the D337A-PML structure. D157A-PML was as stable as the wild-type protein. Nevertheless, it exhibited little lipase and very weak esterase activities. D275A-PML was less stable than the wild-type protein by approximately 5 degrees C in T(1/2). It exhibited weak but significant lipase and esterase activities when compared with the wild-type protein. D337A-PML was also less stable than the wild-type protein by approximately 5 degrees C in T(1/2) but was fully active. These results suggest that the Ca1 site is required to make the active site fully open by anchoring lid 1. The Ca2 and Ca3 sites contribute to the stabilization of PML. The Ca2 site is also required to make PML fully active. Importance of the Ca2+-binding sites in the N-catalytic domain of a family I.3 lipase for activity and stability.,Kuwahara K, Angkawidjaja C, Matsumura H, Koga Y, Takano K, Kanaya S Protein Eng Des Sel. 2008 Dec;21(12):737-44. Epub 2008 Nov 5. PMID:18987131 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lipase

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