Document Type
Preprint
Publication Date
4-1-2007
Journal / Book Title
Archives of Biochemistry and Biophysics
Abstract
The phosphatidylcholine preferring phospholipase C from Bacillus cereus (PC-PLCBc) catalyzes the hydrolysis of phospholipids in the following order of preference: phosphatidylcholine (PC) > phosphatidylethanolamine (PE) > phosphatidylserine (PS). In previous work, mutagenic, kinetic, and crystallographic experiments suggested that varying the amino acids at the 4th, 56th, and 66th positions had a significant influence upon the substrate specificity profile of PC-PLCBc. Here, we report the crystal structures of the native form of several PC-PLCBc variants that exhibited altered substrate specificities for PC, PE, and PS at maximum resolutions of 1.90-2.05 Å. Comparing the structures of these variants to the structure of the wild-type enzyme reveals only minor differences with respect to the number and location of active site water molecules and the side chain conformations of residues at the 4th and 56th positions. These results suggest that subtle changes in steric and electronic properties in the substrate binding site of PC-PLCBc are responsible for the significant changes in substrate selectivity.
DOI
10.1016/j.abb.2007.01.023
Montclair State University Digital Commons Citation
Benfield, Aaron P.; Goodey, Nina; Phillips, Lauren T.; and Martin, Stephen F., "Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants" (2007). Department of Chemistry and Biochemistry Faculty Scholarship and Creative Works. 366.
https://digitalcommons.montclair.edu/chem-biochem-facpubs/366
Published Citation
Published in final edited form as: Arch Biochem Biophys. 2007 April 1; 460(1): 41–47.