2fgn: Difference between revisions
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[[Image:2fgn.gif|left|200px]] | [[Image:2fgn.gif|left|200px]] | ||
'''Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants''' | {{Structure | ||
|PDB= 2fgn |SIZE=350|CAPTION= <scene name='initialview01'>2fgn</scene>, resolution 2.040Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= [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] | |||
|GENE= plc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus]) | |||
}} | |||
'''Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2FGN is a [ | 2FGN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FGN OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17324372 17324372] | ||
[[Category: Bacillus cereus]] | [[Category: Bacillus cereus]] | ||
[[Category: Phospholipase C]] | [[Category: Phospholipase C]] | ||
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[[Category: Martin, S F.]] | [[Category: Martin, S F.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: pc-plcbc protein | [[Category: pc-plcbc protein variant]] | ||
[[Category: substrate specificity]] | [[Category: substrate specificity]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:52:10 2008'' | ||
Revision as of 17:52, 20 March 2008
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| , resolution 2.040Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | plc (Bacillus cereus) | ||||||
| Activity: | Phospholipase C, with EC number 3.1.4.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 1.90-2.05 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.
About this StructureAbout this Structure
2FGN is a Single protein structure of sequence from Bacillus cereus. 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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