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| | <StructureSection load='1olp' size='340' side='right'caption='[[1olp]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1olp' size='340' side='right'caption='[[1olp]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1olp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33455 Atcc 33455]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OLP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1olp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_sardiniense Clostridium sardiniense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OLP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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]] 2.5Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1olp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1olp OCA], [http://pdbe.org/1olp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1olp RCSB], [http://www.ebi.ac.uk/pdbsum/1olp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1olp ProSAT]</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=1olp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1olp OCA], [https://pdbe.org/1olp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1olp RCSB], [https://www.ebi.ac.uk/pdbsum/1olp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1olp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8GCY3_CLOSR Q8GCY3_CLOSR] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 33455]] | + | [[Category: Clostridium sardiniense]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phospholipase C]]
| + | [[Category: Basak AK]] |
| - | [[Category: Basak, A K]] | + | [[Category: Briggs DC]] |
| - | [[Category: Briggs, D C]] | + | |
| - | [[Category: Calcium binding]]
| + | |
| - | [[Category: Gas gangrene determinant]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Membrane binding]]
| + | |
| - | [[Category: Zinc phospholipase c]]
| + | |
| Structural highlights
Function
Q8GCY3_CLOSR
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
Clostridium absonum phospholipase C (Caa) is a 42.7 kDa protein, which shows 60% amino acid sequence identity with the Clostridium perfringens phospholipase C, or alpha-toxin (Cpa), and has been isolated from patients suffering from gas gangrene. We report the cloning and sequencing, purification, characterisation and crystal structure of the Caa enzyme. Caa had twice the phospholipid-hydrolysing (lecithinase) activity, 1.5 times the haemolytic activity and over seven times the activity towards phosphatidylcholine-based liposomes when compared with Cpa. However, the Caa enzyme had a lower activity than Cpa to the free (i.e. not in lipid bilayer) substrate para-nitrophenylphosphorylcholine, towards sphingomyelin-based liposomes and showed half the cytotoxicity. The lethal dose (LD(50)) of Caa in mice was approximately twice that of Cpa. The crystal structure of Caa shows that the 72-93 residue loop is in a conformation different from those of previously determined open-form alpha-toxin structures. This conformational change suggests a role for W84 in membrane binding and a possible route of entry into the active site along a hydrophobic channel created by the re-arrangement of this loop. Overall, the properties of Caa are compatible with a role as a virulence-determinant in gas gangrene caused by C.absonum.
Clostridium absonum alpha-toxin: new insights into clostridial phospholipase C substrate binding and specificity.,Clark GC, Briggs DC, Karasawa T, Wang X, Cole AR, Maegawa T, Jayasekera PN, Naylor CE, Miller J, Moss DS, Nakamura S, Basak AK, Titball RW J Mol Biol. 2003 Oct 31;333(4):759-69. PMID:14568535[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Clark GC, Briggs DC, Karasawa T, Wang X, Cole AR, Maegawa T, Jayasekera PN, Naylor CE, Miller J, Moss DS, Nakamura S, Basak AK, Titball RW. Clostridium absonum alpha-toxin: new insights into clostridial phospholipase C substrate binding and specificity. J Mol Biol. 2003 Oct 31;333(4):759-69. PMID:14568535
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