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2fgn

From Proteopedia

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{{STRUCTURE_2fgn| PDB=2fgn | SCENE= }}
{{STRUCTURE_2fgn| PDB=2fgn | SCENE= }}
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'''Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants'''
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===Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants===
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==Overview==
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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)&gt;phosphatidylethanolamine (PE)&gt;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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(as it appears on PubMed at http://www.pubmed.gov), where 17324372 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17324372}}
==About this Structure==
==About this Structure==
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[[Category: Pc-plcbc protein variant]]
[[Category: Pc-plcbc protein variant]]
[[Category: Substrate specificity]]
[[Category: Substrate specificity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:52:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:08:12 2008''

Revision as of 18:08, 28 July 2008

Image:2fgn.png

Template:STRUCTURE 2fgn

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

Template:ABSTRACT PUBMED 17324372

About this Structure

2FGN is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.

Reference

Structural studies examining the substrate specificity profiles of PC-PLC(Bc) protein variants., Benfield AP, Goodey NM, Phillips LT, Martin SF, Arch Biochem Biophys. 2007 Apr 1;460(1):41-7. Epub 2007 Feb 12. PMID:17324372

Page seeded by OCA on Mon Jul 28 21:08:12 2008

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