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==Crystal structure of the pore forming toxin frac from sea anemone actinia fragacea== | |||
<StructureSection load='3lim' size='340' side='right'caption='[[3lim]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3lim]] is a 6 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=3LIM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LIM FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</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=3lim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lim OCA], [https://pdbe.org/3lim PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lim RCSB], [https://www.ebi.ac.uk/pdbsum/3lim PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lim ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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> | |||
==See Also== | |||
*[[Cytolysin 3D structures|Cytolysin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Actinia fragacea]] | |||
[[Category: Large Structures]] | |||
[[Category: Bellomio A]] | |||
[[Category: Gonzalez-Manas JM]] | |||
[[Category: Guerin DMA]] | |||
[[Category: Mechaly AE]] | |||
[[Category: Morante K]] | |||
Latest revision as of 13:20, 21 February 2024
Crystal structure of the pore forming toxin frac from sea anemone actinia fragaceaCrystal structure of the pore forming toxin frac from sea anemone actinia fragacea
Structural highlights
FunctionACTPC_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.[1] See AlsoReferences
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