2HUC

Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants

2HUC の概要

• エントリーDOI: 10.2210/pdb2huc/pdb
• 関連するPDBエントリー: 2FFZ 2FGN
• 分子名称: Phospholipase C, ZINC ION (3 entities in total)
• 機能のキーワード: plc, bacillus cereus, substrate specificity, e4g, hydrolase
• 由来する生物種: Bacillus cereus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28547.58

構造登録者

Benfield, A.P.,Martin, S.F.,Antikainen, N.M. (登録日: 2006-07-26, 公開日: 2006-08-08, 最終更新日: 2024-02-14)

主引用文献

Benfield, A.P.,Goodey, N.M.,Phillips, L.T.,Martin, S.F.
Structural studies examining the substrate specificity profiles of PC-PLC(Bc) protein variants.
Arch.Biochem.Biophys., 460:41-47, 2007

PubMed Abstract: 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.

PubMed: 17324372
DOI: 10.1016/j.abb.2007.01.023

実験手法

X-RAY DIFFRACTION (1.9 Å)