4wdc: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 1: Line 1:
'''Unreleased structure'''
==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=''>
The entry 4wdc is ON HOLD  until Paper Publication
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4wdc]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WDC FirstGlance]. <br>
Authors: Caaveiro, J.M.M., Morante, K., Tsumoto, K.
</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=4wdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wdc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wdc RCSB], [http://www.ebi.ac.uk/pdbsum/4wdc PDBsum]</span></td></tr>
 
</table>
Description: High-resolution crystal structure of water-soluble FraC (mutation F16P)
== Function ==
[[Category: Unreleased Structures]]
[[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> 
[[Category: Caaveiro, J.M.M]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caaveiro, J M.M]]
[[Category: Morante, K]]
[[Category: Morante, K]]
[[Category: Tsumoto, K]]
[[Category: Tsumoto, K]]
[[Category: Actinoporin]]
[[Category: Cholesterol]]
[[Category: Lipid packing]]
[[Category: Pore forming toxin]]
[[Category: Protein-lipid interaction]]

Revision as of 15:15, 18 March 2015

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. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, RCSB, PDBsum

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]

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

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=4wdc&oldid=2385958"