8yzo | pdb_00008yzo

Crystal structural analysis of PaL mutant L297M

spinqualitylabelsall models 8yzo, resolution 1.77Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8yzo is a 1 chain structure with sequence from Pseudomonas alcaligenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.769Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H9MZI2_PSEAC Publication Abstract from PubMed The Pseudomonas aeruginosa lipase PaL catalyzes the stereoselective hydrolysis of menthyl propionate to produce L-menthol. The lack of a three-dimensional structure of PaL has so far prevented a detailed understanding of its stereoselective reaction mechanism. Here, the crystal structure of PaL was determined at a resolution of 1.80 A by single-wavelength anomalous diffraction. In the apo-PaL structure, the catalytic His302 is located in a long loop on the surface that is solvent exposed. His302 is distant from the other two catalytic residues, Asp274 and Ser164. This configuration of catalytic residues is unusual for lipases. Using metadynamics simulations, we observed that the enzyme undergoes a significant conformational change upon ligand binding. We also explored the catalytic and stereoselectivity mechanisms of PaL by all-atom molecular dynamics simulations. These findings could guide the engineering of PaL with an improved diastereoselectivity for L-menthol production. Crystal structure of lipase from Pseudomonas aeruginosa reveals an unusual catalytic triad conformation.,Xu G, Guo H, Yu Z, Wang S, Shen D, Yang L, Wu J, Chen B, Yu H Structure. 2024 Sep 5;32(9):1454-1464.e3. doi: 10.1016/j.str.2024.06.014. Epub , 2024 Jul 17. PMID:39025068 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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