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. Author manuscript; available in PMC: 2011 Mar 9.
Published in final edited form as: Biochemistry. 2010 Mar 9;49(9):1931–1942. doi: 10.1021/bi9021268

Figure 4.

Figure 4

Mesh showing water-accessible regions in the active sites of wild-type PFE and L29P with the modeled tetrahedral intermediate for the acetylation of active site serine by ethyl acetate (Td1). (A) The alcohol pocket accommodates the ethyl group of the tetrahedral intermediate and could also accept a longer alcohol, but not larger acyl groups. The acyl pocket of wild-type PFE is small while the alcohol pocket is larger, as shown on the diagram on the right side. (B) The leucine to proline substitution shifts the main chain W28 carbonyl which pinches off the alcohol pocket. The ethyl group is forced to adopt an unfavorable conformation in the enlarged acyl pocket caused by a shift in the indole ring of W28. A diagram on the right shows that the acyl pocket of L29P is larger than the alcohol pocket. The mesh shows regions accessible to a sphere with a radius of 1.4 Å, which models a water molecule. Water molecules were removed before modeling the mesh regions.