کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1927237 1536506 2007 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Structural studies examining the substrate specificity profiles of PC-PLCBc protein variants
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Structural studies examining the substrate specificity profiles of PC-PLCBc protein variants
چکیده انگلیسی

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volume 460, Issue 1, 1 April 2007, Pages 41–47
نویسندگان
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