2fgn: Difference between revisions

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 <StructureSection load='2fgn' size='340' side='right'caption='[[2fgn]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2fgn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FGN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2fgn]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FGN FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ffz|2ffz]], [[2fgm|2fgm]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">plc ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 ATCC 14579])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phospholipase_C Phospholipase C], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3] </span></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fgn OCA], [https://pdbe.org/2fgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fgn RCSB], [https://www.ebi.ac.uk/pdbsum/2fgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fgn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PHLC_BACCE PHLC_BACCE]] Required, with sphingomyelinase, to effect target cell lysis (hemolysis).
+[https://www.uniprot.org/uniprot/PHLC_BACCE PHLC_BACCE] Required, with sphingomyelinase, to effect target cell lysis (hemolysis).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fgn ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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<ref>PMID:17324372</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2fgn" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Phospholipase C|Phospholipase C]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 14579]]
+[[Category: Bacillus cereus]]
 [[Category: Large Structures]]
-[[Category: Phospholipase C]]
+[[Category: Benfield AP]]
-[[Category: Benfield, A P]]
+[[Category: Martin SF]]
-[[Category: Martin, S F]]
-[[Category: Hydrolase]]
-[[Category: Pc-plcbc protein variant]]
-[[Category: Substrate specificity]]