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4tso

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<StructureSection load='4tso' size='340' side='right'caption='[[4tso]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='4tso' size='340' side='right'caption='[[4tso]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4tso]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Actfr Actfr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TSO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TSO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4tso]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinia_fragacea Actinia fragacea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TSO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HXG:1,2-DIHEXANOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>HXG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tsl|4tsl]], [[4tsn|4tsn]], [[4tsp|4tsp]], [[4tsq|4tsq]], [[4tsy|4tsy]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HXG:1,2-DIHEXANOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>HXG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=4tso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tso OCA], [http://pdbe.org/4tso PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tso RCSB], [http://www.ebi.ac.uk/pdbsum/4tso PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tso ProSAT]</span></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=4tso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tso OCA], [https://pdbe.org/4tso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tso RCSB], [https://www.ebi.ac.uk/pdbsum/4tso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tso ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ACTPC_ACTFR ACTPC_ACTFR]] Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of several monomers.<ref>PMID:19563820</ref>
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[https://www.uniprot.org/uniprot/ACTPC_ACTFR ACTPC_ACTFR] Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of several monomers.<ref>PMID:19563820</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4tso" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4tso" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Cytolysin 3D structures|Cytolysin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Actfr]]
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[[Category: Actinia fragacea]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Caaveiro, J M.M]]
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[[Category: Caaveiro JMM]]
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[[Category: Tanaka, K]]
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[[Category: Tanaka K]]
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[[Category: Tsumoto, K]]
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[[Category: Tsumoto K]]
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[[Category: Actinoporin]]
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[[Category: Lipid-protein interaction]]
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[[Category: Membrane lipid]]
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[[Category: Phosphocholine]]
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[[Category: Pore-forming toxin]]
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[[Category: Toxin]]
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Current revision

Crystal structure of FraC with DHPC bound (crystal form I)

PDB ID 4tso

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