2fgn: Difference between revisions

Revision as of 03:52, 4 May 2008

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 Page seeded by OCA on Sun May 4 03:52:19 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 [[Image:2fgn.gif|left|200px]]
- {{Structure
+<!--
-|PDB= 2fgn |SIZE=350|CAPTION= <scene name='initialview01'>2fgn</scene>, resolution 2.040&Aring;
+The line below this paragraph, containing "STRUCTURE_2fgn", creates the "Structure Box" on the page.
-|SITE=
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
-|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-|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>
+or leave the SCENE parameter empty for the default display.
-|GENE= plc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus])
+-->
-|DOMAIN=
+{{STRUCTURE_2fgn|  PDB=2fgn  |  SCENE=  }}
-|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>
-}}
 '''Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants'''
@@ Line 28: / Line 25: @@
 [[Category: Benfield, A P.]]
 [[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 Sun May  4 03:52:19 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:02:31 2008''