2huc: Difference between revisions

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-[[Image:2huc.gif|left|200px]]
-<!--
+==Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants==
-The line below this paragraph, containing "STRUCTURE_2huc", creates the "Structure Box" on the page.
+<StructureSection load='2huc' size='340' side='right'caption='[[2huc]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2huc]] 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=2HUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HUC FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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>
-{{STRUCTURE_2huc|  PDB=2huc  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2huc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2huc OCA], [https://pdbe.org/2huc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2huc RCSB], [https://www.ebi.ac.uk/pdbsum/2huc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2huc ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hu/2huc_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2huc ConSurf].
+<div style="clear:both"></div>
-'''Structural Studies Examining the Substrate Specificity Profiles of PC-PLCBc Protein Variants'''
+==See Also==
+*[[Phospholipase C|Phospholipase C]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
-==About this Structure==
-HUC 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=2HUC OCA].
-==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://www.ncbi.nlm.nih.gov/pubmed/17324372 17324372]
-[[Category: Bacillus cereus]]
-[[Category: Phospholipase C]]
-[[Category: Single protein]]
-[[Category: Antikainen, N M.]]
-[[Category: Benfield, A P.]]
-[[Category: Martin, S F.]]
 [[Category: Bacillus cereus]]
-[[Category: E4g]]
+[[Category: Large Structures]]
-[[Category: Plc]]
+[[Category: Antikainen NM]]
-[[Category: Substrate specificity]]
+[[Category: Benfield AP]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:43:18 2008''
+[[Category: Martin SF]]