4tsq: Difference between revisions

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 ==Crystal structure of FraC with DHPC bound (crystal form III)==
-<StructureSection load='4tsq' size='340' side='right' caption='[[4tsq]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+<StructureSection load='4tsq' size='340' side='right'caption='[[4tsq]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4tsq]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TSQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TSQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4tsq]] 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=4TSQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TSQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HXG:1,2-DIHEXANOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>HXG</scene>, <scene name='pdbligand=PC:PHOSPHOCHOLINE'>PC</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vwi|3vwi]], [[3wp9|3wp9]], [[4tsl|4tsl]], [[4tsn|4tsn]], [[4tso|4tso]], [[4tsp|4tsp]], [[4tsy|4tsy]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HXG:1,2-DIHEXANOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>HXG</scene>, <scene name='pdbligand=PC:PHOSPHOCHOLINE'>PC</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></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=4tsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tsq OCA], [http://pdbe.org/4tsq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tsq RCSB], [http://www.ebi.ac.uk/pdbsum/4tsq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tsq ProSAT]</span></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=4tsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tsq OCA], [https://pdbe.org/4tsq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tsq RCSB], [https://www.ebi.ac.uk/pdbsum/4tsq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tsq 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 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 4tsq" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cytolysin 3D structures|Cytolysin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Caaveiro, J M.M]]
+[[Category: Actinia fragacea]]
-[[Category: Tanaka, K]]
+[[Category: Large Structures]]
-[[Category: Tsumoto, K]]
+[[Category: Caaveiro JMM]]
-[[Category: Actinoporin pore-forming toxin]]
+[[Category: Tanaka K]]
-[[Category: Lipid-protein interaction]]
+[[Category: Tsumoto K]]
-[[Category: Membrane lipid]]
-[[Category: Phosphocholine]]
-[[Category: Toxin]]