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[[Image:1p6d.jpg|left|200px]]


{{Structure
==STRUCTURE OF THE D55N MUTANT OF PHOSPHOLIPASE C FROM BACILLUS CEREUS IN COMPLEX WITH (3S)-3,4,DI-N-HEXANOYLOXYBUTYL-1-PHOSPHOCHOLINE==
|PDB= 1p6d |SIZE=350|CAPTION= <scene name='initialview01'>1p6d</scene>, resolution 2.0&Aring;
<StructureSection load='1p6d' size='340' side='right'caption='[[1p6d]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=3PC:(3S)-3,4-DI-N-HEXANOYLOXYBUTYL-1-PHOSPHOCHOLINE'>3PC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
<table><tr><td colspan='2'>[[1p6d]] 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=1P6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P6D FirstGlance]. <br>
|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>
</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&#8491;</td></tr>
|GENE= plc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PC:(3S)-3,4-DI-N-HEXANOYLOXYBUTYL-1-PHOSPHOCHOLINE'>3PC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p6d OCA], [https://pdbe.org/1p6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p6d RCSB], [https://www.ebi.ac.uk/pdbsum/1p6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p6d ProSAT]</span></td></tr>
|RELATEDENTRY=[[1ah7|1AH7]], [[1p5x|1P5X]], [[1p6e|1P6E]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p6d OCA], [http://www.ebi.ac.uk/pdbsum/1p6d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p6d RCSB]</span>
== 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/p6/1p6d_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=1p6d ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Because mutations of the ionizable Asp at position 55 of the phosphatidylcholine preferring phospholipase C from Bacillus cereus (PLC(Bc)) to a non-ionizable Asn generate a mutant enzyme (D55N) with 10(4)-fold lower catalytic activity than the wild-type enzyme, we tentatively identified Asp55 as the general base for the enzymatic reaction. To eliminate the alternate possibility that Asp55 is a structurally important amino acid, the X-ray structures of unbound D55N and complexes of D55N with two non-hydrolyzable substrate analogues have been solved and refined to 2.0, 2.0, and 2.3A, respectively. The structures of unbound wild-type PLC(Bc) and a wild-type PLC(Bc)-complex with a non-hydrolyzable substrate analogue do not change significantly as a result of replacing Asp55 with Asn. These observations demonstrate that Asp55 is not critical for the structural integrity of the enzyme and support the hypothesis that Asp55 is the general base in the PLC(Bc)-catalyzed hydrolysis of phospholipids.


'''STRUCTURE OF THE D55N MUTANT OF PHOSPHOLIPASE C FROM BACILLUS CEREUS IN COMPLEX WITH (3S)-3,4,DI-N-HEXANOYLOXYBUTYL-1-PHOSPHOCHOLINE'''
Using X-ray crystallography of the Asp55Asn mutant of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus to support the mechanistic role of Asp55 as the general base.,Antikainen NM, Monzingo AF, Franklin CL, Robertus JD, Martin SF Arch Biochem Biophys. 2003 Sep 1;417(1):81-6. PMID:12921783<ref>PMID:12921783</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1p6d" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Because mutations of the ionizable Asp at position 55 of the phosphatidylcholine preferring phospholipase C from Bacillus cereus (PLC(Bc)) to a non-ionizable Asn generate a mutant enzyme (D55N) with 10(4)-fold lower catalytic activity than the wild-type enzyme, we tentatively identified Asp55 as the general base for the enzymatic reaction. To eliminate the alternate possibility that Asp55 is a structurally important amino acid, the X-ray structures of unbound D55N and complexes of D55N with two non-hydrolyzable substrate analogues have been solved and refined to 2.0, 2.0, and 2.3A, respectively. The structures of unbound wild-type PLC(Bc) and a wild-type PLC(Bc)-complex with a non-hydrolyzable substrate analogue do not change significantly as a result of replacing Asp55 with Asn. These observations demonstrate that Asp55 is not critical for the structural integrity of the enzyme and support the hypothesis that Asp55 is the general base in the PLC(Bc)-catalyzed hydrolysis of phospholipids.
*[[Phospholipase C|Phospholipase C]]
 
== References ==
==About this Structure==
<references/>
1P6D 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=1P6D OCA].
__TOC__
 
</StructureSection>
==Reference==
Using X-ray crystallography of the Asp55Asn mutant of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus to support the mechanistic role of Asp55 as the general base., Antikainen NM, Monzingo AF, Franklin CL, Robertus JD, Martin SF, Arch Biochem Biophys. 2003 Sep 1;417(1):81-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12921783 12921783]
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
[[Category: Phospholipase C]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Antikainen NM]]
[[Category: Antikainen, N M.]]
[[Category: Franklin CL]]
[[Category: Franklin, C L.]]
[[Category: Martin SF]]
[[Category: Martin, S F.]]
[[Category: Monzingo AF]]
[[Category: Monzingo, A F.]]
[[Category: Robertus JD]]
[[Category: Robertus, J D.]]
[[Category: tri zn2+ metal core]]
 
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