2fgn: Difference between revisions
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|PDB= 2fgn |SIZE=350|CAPTION= <scene name='initialview01'>2fgn</scene>, resolution 2.040Å | |PDB= 2fgn |SIZE=350|CAPTION= <scene name='initialview01'>2fgn</scene>, resolution 2.040Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= plc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus]) | |GENE= plc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2ffz|2FFZ]], [[2fgm|2FGM]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fgn OCA], [http://www.ebi.ac.uk/pdbsum/2fgn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fgn RCSB]</span> | |||
}} | }} | ||
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[[Category: Benfield, A P.]] | [[Category: Benfield, A P.]] | ||
[[Category: Martin, S F.]] | [[Category: Martin, S F.]] | ||
[[Category: pc-plcbc protein variant]] | [[Category: pc-plcbc protein variant]] | ||
[[Category: substrate specificity]] | [[Category: substrate specificity]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:02:31 2008'' | ||
Revision as of 03:02, 31 March 2008
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| , resolution 2.040Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | plc (Bacillus cereus) | ||||||
| Activity: | Phospholipase C, with EC number 3.1.4.3 | ||||||
| Related: | 2FFZ, 2FGM
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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