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==STRUCTURE OF THE D55N MUTANT OF PHOSPHOLIPASE C FROM BACILLUS CEREUS IN COMPLEX WITH 1,2-DI-N-PENTANOYL-SN-GLYCERO-3-DITHIOPHOSPHOCHOLINE==
==STRUCTURE OF THE D55N MUTANT OF PHOSPHOLIPASE C FROM BACILLUS CEREUS IN COMPLEX WITH 1,2-DI-N-PENTANOYL-SN-GLYCERO-3-DITHIOPHOSPHOCHOLINE==
<StructureSection load='1p6e' size='340' side='right' caption='[[1p6e]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1p6e' size='340' side='right'caption='[[1p6e]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1p6e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P6E FirstGlance]. <br>
<table><tr><td colspan='2'>[[1p6e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P6E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1P6E FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PC5:1,2-DI-N-PENTANOYL-SN-GLYCERO-3-DITHIOPHOSPHOCHOLINE'>PC5</scene>, <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=PC5:1,2-DI-N-PENTANOYL-SN-GLYCERO-3-DITHIOPHOSPHOCHOLINE'>PC5</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ah7|1ah7]], [[1p5x|1p5x]], [[1p6d|1p6d]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ah7|1ah7]], [[1p5x|1p5x]], [[1p6d|1p6d]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PLC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 ATCC 14579])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PLC ([http://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'>[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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p6e OCA], [http://pdbe.org/1p6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p6e RCSB], [http://www.ebi.ac.uk/pdbsum/1p6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p6e ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1p6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p6e OCA], [http://pdbe.org/1p6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p6e RCSB], [http://www.ebi.ac.uk/pdbsum/1p6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p6e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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</div>
</div>
<div class="pdbe-citations 1p6e" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1p6e" 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 10:23, 9 December 2020

STRUCTURE OF THE D55N MUTANT OF PHOSPHOLIPASE C FROM BACILLUS CEREUS IN COMPLEX WITH 1,2-DI-N-PENTANOYL-SN-GLYCERO-3-DITHIOPHOSPHOCHOLINESTRUCTURE OF THE D55N MUTANT OF PHOSPHOLIPASE C FROM BACILLUS CEREUS IN COMPLEX WITH 1,2-DI-N-PENTANOYL-SN-GLYCERO-3-DITHIOPHOSPHOCHOLINE

Structural highlights

1p6e is a 1 chain structure with sequence from Atcc 14579. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:PLC (ATCC 14579)
Activity:Phospholipase C, with EC number 3.1.4.3
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Antikainen NM, Monzingo AF, Franklin CL, Robertus JD, Martin SF. 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. Arch Biochem Biophys. 2003 Sep 1;417(1):81-6. PMID:12921783

1p6e, resolution 2.30Å

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