4wdc: Difference between revisions
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==High-resolution crystal structure of water-soluble FraC (mutation F16P)== | |||
<StructureSection load='4wdc' size='340' side='right'caption='[[4wdc]], [[Resolution|resolution]] 1.29Å' 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]] 1.29Å</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> | |||
==See Also== | |||
*[[Cytolysin 3D structures|Cytolysin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[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
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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