2ffz: Difference between revisions
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==Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants== | ==Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants== | ||
<StructureSection load='2ffz' size='340' side='right' caption='[[2ffz]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='2ffz' size='340' side='right'caption='[[2ffz]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ffz]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2ffz]] 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=2FFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FFZ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </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 ([ | <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'>[ | <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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ffz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ffz OCA], [https://pdbe.org/2ffz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ffz RCSB], [https://www.ebi.ac.uk/pdbsum/2ffz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ffz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/PHLC_BACCE PHLC_BACCE]] Required, with sphingomyelinase, to effect target cell lysis (hemolysis). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/2ffz_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/2ffz_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2ffz" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2ffz" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Phospholipase C|Phospholipase C]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 14579]] | [[Category: Atcc 14579]] | ||
[[Category: Large Structures]] | |||
[[Category: Phospholipase C]] | [[Category: Phospholipase C]] | ||
[[Category: Antikainen, N M]] | [[Category: Antikainen, N M]] | ||
Revision as of 10:16, 24 February 2021
Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein VariantsStructural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants
Structural highlights
Function[PHLC_BACCE] Required, with sphingomyelinase, to effect target cell lysis (hemolysis). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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