4wdc: Difference between revisions

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'''Unreleased structure'''


The entry 4wdc is ON HOLD  until Paper Publication
==High-resolution crystal structure of water-soluble FraC (mutation F16P)==
<StructureSection load='4wdc' size='340' side='right'caption='[[4wdc]], [[Resolution|resolution]] 1.29&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wdc]] is a 1 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=4WDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WDC 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]] 1.29&#8491;</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=4wdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wdc OCA], [https://pdbe.org/4wdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wdc RCSB], [https://www.ebi.ac.uk/pdbsum/4wdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wdc 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>


Authors: Caaveiro, J.M.M., Morante, K., Tsumoto, K.
==See Also==
 
*[[Cytolysin 3D structures|Cytolysin 3D structures]]
Description: High-resolution crystal structure of water-soluble FraC (mutation F16P)
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Caaveiro, J.M.M]]
__TOC__
[[Category: Morante, K]]
</StructureSection>
[[Category: Tsumoto, K]]
[[Category: Actinia fragacea]]
[[Category: Large Structures]]
[[Category: Caaveiro JMM]]
[[Category: Morante K]]
[[Category: Tsumoto K]]

Latest revision as of 12:01, 20 March 2024

High-resolution crystal structure of water-soluble FraC (mutation F16P)High-resolution crystal structure of water-soluble FraC (mutation F16P)

Structural highlights

4wdc is a 1 chain structure with sequence from Actinia fragacea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.29Å
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]

See Also

References

  1. 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

4wdc, resolution 1.29Å

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