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4tsl

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Revision as of 10:53, 15 March 2023

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

Structural highlights

4tsl is a 2 chain structure with sequence from Actinia fragacea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1]

Publication Abstract from PubMed

Pore-forming toxins (PFT) are water-soluble proteins that possess the remarkable ability to self-assemble on the membrane of target cells, where they form pores causing cell damage. Here, we elucidate the mechanism of action of the haemolytic protein fragaceatoxin C (FraC), a alpha-barrel PFT, by determining the crystal structures of FraC at four different stages of the lytic mechanism, namely the water-soluble state, the monomeric lipid-bound form, an assembly intermediate and the fully assembled transmembrane pore. The structure of the transmembrane pore exhibits a unique architecture composed of both protein and lipids, with some of the lipids lining the pore wall, acting as assembly cofactors. The pore also exhibits lateral fenestrations that expose the hydrophobic core of the membrane to the aqueous environment. The incorporation of lipids from the target membrane within the structure of the pore provides a membrane-specific trigger for the activation of a haemolytic toxin.

Structural basis for self-assembly of a cytolytic pore lined by protein and lipid.,Tanaka K, Caaveiro JM, Morante K, Gonzalez-Manas JM, Tsumoto K Nat Commun. 2015 Feb 26;6:6337. doi: 10.1038/ncomms7337. PMID:25716479^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bellomio A, Morante K, Barlic A, Gutierrez-Aguirre I, Viguera AR, Gonzalez-Manas JM. Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea. Toxicon. 2009 Nov;54(6):869-80. doi: 10.1016/j.toxicon.2009.06.022. Epub 2009 Jun, 27. PMID:19563820 doi:10.1016/j.toxicon.2009.06.022
↑ Tanaka K, Caaveiro JM, Morante K, Gonzalez-Manas JM, Tsumoto K. Structural basis for self-assembly of a cytolytic pore lined by protein and lipid. Nat Commun. 2015 Feb 26;6:6337. doi: 10.1038/ncomms7337. PMID:25716479 doi:http://dx.doi.org/10.1038/ncomms7337

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4tsl"

Categories: Actinia fragacea | Large Structures | Caaveiro JMM | Tanaka K | Tsumoto K

@@ Line 3: / Line 3: @@
 <StructureSection load='4tsl' size='340' side='right'caption='[[4tsl]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4tsl]] 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=4TSL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TSL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4tsl]] 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=4TSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TSL FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PC:PHOSPHOCHOLINE'>PC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</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=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PC:PHOSPHOCHOLINE'>PC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vwi|3vwi]], [[3w9p|3w9p]], [[4tsn|4tsn]], [[4tso|4tso]], [[4tsp|4tsp]], [[4tsq|4tsq]], [[4tsy|4tsy]]</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=4tsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tsl OCA], [https://pdbe.org/4tsl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tsl RCSB], [https://www.ebi.ac.uk/pdbsum/4tsl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tsl ProSAT]</span></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=4tsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tsl OCA], [http://pdbe.org/4tsl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tsl RCSB], [http://www.ebi.ac.uk/pdbsum/4tsl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tsl ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[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;">
 == Publication Abstract from PubMed ==
@@ Line 26: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Actfr]]
+[[Category: Actinia fragacea]]
 [[Category: Large Structures]]
-[[Category: Caaveiro, J M.M]]
+[[Category: Caaveiro JMM]]
-[[Category: Tanaka, K]]
+[[Category: Tanaka K]]
-[[Category: Tsumoto, K]]
+[[Category: Tsumoto K]]
-[[Category: Actinoporin]]
-[[Category: Lipid-protein interaction]]
-[[Category: Membrane lipid]]
-[[Category: Phosphocholine]]
-[[Category: Pore-forming toxin]]
-[[Category: Toxin]]

4tsl

From Proteopedia

Revision as of 10:53, 15 March 2023

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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