2FGN: Structural Studies Examining The Substrate Specificity Profiles Of Pc- Plcbc Protein Variants

The phosphatidylcholine preferring phospholipase C from Bacillus cereus (PC-PLC(Bc)) 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-PLC(Bc). Here, we report the crystal structures of the native form of several PC-PLC(Bc) variants that exhibited altered substrate specificities for PC, PE, and PS at maximum resolutions of 1.90-2.05 Angstrom. 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-PLC(Bc) are responsible for the significant changes in substrate selectivity.
PDB ID: 2FGNDownload
MMDB ID: 38261
PDB Deposition Date: 2005/12/22
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.04  Å
Source Organism:
Similar Structures:
Biological Unit for 2FGN: monomeric; determined by author
Molecular Components in 2FGN
Label Count Molecule
Protein (1 molecule)
Phospholipase C
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB