3i5v
From Proteopedia
(Difference between revisions)
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<StructureSection load='3i5v' size='340' side='right'caption='[[3i5v]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3i5v' size='340' side='right'caption='[[3i5v]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3i5v]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3i5v]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_RN4220 Staphylococcus aureus subsp. aureus RN4220]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I5V FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGA:DIACYL+GLYCEROL'>DGA</scene></td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3i5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i5v OCA], [https://pdbe.org/3i5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i5v RCSB], [https://www.ebi.ac.uk/pdbsum/3i5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i5v 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=3i5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i5v OCA], [https://pdbe.org/3i5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i5v RCSB], [https://www.ebi.ac.uk/pdbsum/3i5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i5v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PHLC_STAAU PHLC_STAAU] Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Beta-hemolysin is a phospholipase C with specific activity toward sphingomyelins. Has a high specificity for sphingomyelin, hydrolyzes lysophosphatidylcholine at a much lower rate, but has no activity towards phosphatidylcholine, phosphatidylethanolamine, or phosphatidylserine (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=3i5v ConSurf]. | </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=3i5v ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Beta toxin is a neutral sphingomyelinase secreted by certain strains of Staphylococcus aureus. This virulence factor lyses erythrocytes in order to evade the host immune system as well as scavenge nutrients. The structure of beta toxin was determined at 2.4-A resolution using crystals that were merohedrally twinned. This structure is similar to that of the sphingomyelinases of Listeria ivanovii and Bacillus cereus. Beta toxin belongs to the DNase I folding superfamily; in addition to sphingomyelinases, the proteins most structurally related to beta toxin include human endonuclease HAP1, Escherichia coli endonuclease III, bovine pancreatic DNase I, and the endonuclease domain of TRAS1 from Bombyx mori. Our biological assays demonstrated for the first time that beta toxin kills proliferating human lymphocytes. Structure-directed active site mutations show that biological activities, including hemolysis and lymphotoxicity, are due to the sphingomyelinase activity of the enzyme. | ||
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| - | Structure and biological activities of beta toxin from Staphylococcus aureus.,Huseby M, Shi K, Brown CK, Digre J, Mengistu F, Seo KS, Bohach GA, Schlievert PM, Ohlendorf DH, Earhart CA J Bacteriol. 2007 Dec;189(23):8719-26. Epub 2007 Sep 14. PMID:17873030<ref>PMID:17873030</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3i5v" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Hemolysin 3D structures|Hemolysin 3D structures]] | *[[Hemolysin 3D structures|Hemolysin 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Staphylococcus aureus | + | [[Category: Staphylococcus aureus subsp. aureus RN4220]] |
| - | [[Category: Huseby | + | [[Category: Huseby M]] |
| - | [[Category: Kruse | + | [[Category: Kruse AC]] |
| - | [[Category: Ohlendorf | + | [[Category: Ohlendorf DH]] |
| - | [[Category: Shi | + | [[Category: Shi K]] |
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Revision as of 06:39, 3 April 2024
Crystal structure of beta toxin 275-280 from Staphylococcus aureus
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