2ffz: Difference between revisions
New page: left|200px<br /><applet load="2ffz" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ffz, resolution 2.050Å" /> '''Structural Studies ... |
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[[Image:2ffz.gif|left|200px]]<br /><applet load="2ffz" size=" | [[Image:2ffz.gif|left|200px]]<br /><applet load="2ffz" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2ffz, resolution 2.050Å" /> | caption="2ffz, resolution 2.050Å" /> | ||
'''Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants'''<br /> | '''Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2FFZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phospholipase_C Phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3] Full crystallographic information is available from [http:// | 2FFZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phospholipase_C Phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FFZ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: substrate specificity]] | [[Category: substrate specificity]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:29:59 2008'' | ||
Revision as of 16:30, 23 January 2008
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Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants
OverviewOverview
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 1.90-2.05A. 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.
About this StructureAbout this Structure
2FFZ is a Single protein structure of sequence from Bacillus cereus with as ligand. Active as Phospholipase C, with EC number 3.1.4.3 Full crystallographic information is available from OCA.
ReferenceReference
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
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