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PDBsum entry 2ffz
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References listed in PDB file
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Key reference
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Title
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Structural studies examining the substrate specificity profiles of pc-Plc(bc) protein variants.
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Authors
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A.P.Benfield,
N.M.Goodey,
L.T.Phillips,
S.F.Martin.
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Ref.
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Arch Biochem Biophys, 2007,
460,
41-47.
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PubMed id
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Abstract
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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.
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