4cdb: Difference between revisions
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==Crystal structure of listeriolysin O== | ==Crystal structure of listeriolysin O== | ||
<StructureSection load='4cdb' size='340' side='right' caption='[[4cdb]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='4cdb' size='340' side='right'caption='[[4cdb]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
[[4cdb]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4cdb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CDB FirstGlance]. <br> | ||
<b> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></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=4cdb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cdb OCA], [https://pdbe.org/4cdb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cdb RCSB], [https://www.ebi.ac.uk/pdbsum/4cdb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cdb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H3GD84_LISM4 A0A0H3GD84_LISM4] A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is required for binding to host membranes, membrane insertion and pore formation; cholesterol binding is mediated by a Thr-Leu pair in the C-terminus. Can be reversibly inactivated by oxidation.[RuleBase:RU364025] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Listeriolysin O (LLO) is an essential virulence factor of Listeria monocytogenes that causes listeriosis. Listeria monocytogenes owes its ability to live within cells to the pH- and temperature-dependent pore-forming activity of LLO, which is unique among cholesterol-dependent cytolysins. LLO enables the bacteria to cross the phagosomal membrane and is also involved in activation of cellular processes, including the modulation of gene expression or intracellular Ca(2+) oscillations. Neither the pore-forming mechanism nor the mechanisms triggering the signalling processes in the host cell are known in detail. Here, we report the crystal structure of LLO, in which we identified regions important for oligomerization and pore formation. Mutants were characterized by determining their haemolytic and Ca(2+) uptake activity. We analysed the pore formation of LLO and its variants on erythrocyte ghosts by electron microscopy and show that pore formation requires precise interface interactions during toxin oligomerization on the membrane. | |||
Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation.,Koster S, van Pee K, Hudel M, Leustik M, Rhinow D, Kuhlbrandt W, Chakraborty T, Yildiz O Nat Commun. 2014 Apr 22;5:3690. doi: 10.1038/ncomms4690. PMID:24751541<ref>PMID:24751541</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4cdb" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytolysin 3D structures|Cytolysin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Listeria monocytogenes]] | [[Category: Listeria monocytogenes]] | ||
[[Category: Koester | [[Category: Koester S]] | ||
[[Category: Yildiz | [[Category: Yildiz O]] | ||
Latest revision as of 15:08, 20 December 2023
Crystal structure of listeriolysin OCrystal structure of listeriolysin O
Structural highlights
FunctionA0A0H3GD84_LISM4 A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is required for binding to host membranes, membrane insertion and pore formation; cholesterol binding is mediated by a Thr-Leu pair in the C-terminus. Can be reversibly inactivated by oxidation.[RuleBase:RU364025] Publication Abstract from PubMedListeriolysin O (LLO) is an essential virulence factor of Listeria monocytogenes that causes listeriosis. Listeria monocytogenes owes its ability to live within cells to the pH- and temperature-dependent pore-forming activity of LLO, which is unique among cholesterol-dependent cytolysins. LLO enables the bacteria to cross the phagosomal membrane and is also involved in activation of cellular processes, including the modulation of gene expression or intracellular Ca(2+) oscillations. Neither the pore-forming mechanism nor the mechanisms triggering the signalling processes in the host cell are known in detail. Here, we report the crystal structure of LLO, in which we identified regions important for oligomerization and pore formation. Mutants were characterized by determining their haemolytic and Ca(2+) uptake activity. We analysed the pore formation of LLO and its variants on erythrocyte ghosts by electron microscopy and show that pore formation requires precise interface interactions during toxin oligomerization on the membrane. Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation.,Koster S, van Pee K, Hudel M, Leustik M, Rhinow D, Kuhlbrandt W, Chakraborty T, Yildiz O Nat Commun. 2014 Apr 22;5:3690. doi: 10.1038/ncomms4690. PMID:24751541[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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