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6mrt

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12-meric ClyA pore complex

6mrt, resolution 2.80Å

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 <SX load='6mrt' size='340' side='right' viewer='molstar' caption='[[6mrt]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6mrt]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MRT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MRT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6mrt]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MRT FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hlyE, clyA, hpr, sheA, ycgD, b1182, JW5181 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8&#8491;</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=6mrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mrt OCA], [http://pdbe.org/6mrt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mrt RCSB], [http://www.ebi.ac.uk/pdbsum/6mrt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mrt 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=6mrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mrt OCA], [https://pdbe.org/6mrt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mrt RCSB], [https://www.ebi.ac.uk/pdbsum/6mrt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mrt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HLYE_ECOLI HLYE_ECOLI]] Toxin, which has some hemolytic activity towards mammalian cells. Acts by forming a pore-like structure upon contact with mammalian cells.<ref>PMID:14532000</ref>
+[https://www.uniprot.org/uniprot/HLYE_ECOLI HLYE_ECOLI] Toxin, which has some hemolytic activity towards mammalian cells. Acts by forming a pore-like structure upon contact with mammalian cells.<ref>PMID:14532000</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Pore-forming proteins (PFPs) represent a functionally important protein family, that are found in organisms from viruses to humans. As a major branch of PFPs, bacteria pore-forming toxins (PFTs) permeabilize membranes and usually cause the death of target cells. E. coli hemolysin ClyA is the first member with the pore complex structure solved among alpha-PFTs, employing alpha-helices as transmembrane elements. ClyA is proposed to form pores composed of various numbers of protomers. With high-resolution cryo-EM structures, we observe that ClyA pore complexes can exist as newly confirmed oligomers of a tridecamer and a tetradecamer, at estimated resolutions of 3.2 A and 4.3 A, respectively. The 2.8 A cryo-EM structure of a dodecamer dramatically improves the existing structural model. Structural analysis indicates that protomers from distinct oligomers resemble each other and neighboring protomers adopt a conserved interaction mode. We also show a stabilized intermediate state of ClyA during the transition process from soluble monomers to pore complexes. Unexpectedly, even without the formation of mature pore complexes, ClyA can permeabilize membranes and allow leakage of particles less than ~400 Daltons. In addition, we are the first to show that ClyA forms pore complexes in the presence of cholesterol within artificial liposomes. These findings provide new mechanistic insights into the dynamic process of pore assembly for the prototypical alpha-PFT ClyA.
-High-resolution cryo-EM structures of the E. coli hemolysin ClyA oligomers.,Peng W, de Souza Santos M, Li Y, Tomchick DR, Orth K PLoS One. 2019 May 2;14(5):e0213423. doi: 10.1371/journal.pone.0213423., eCollection 2019. PMID:31048915<ref>PMID:31048915</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6mrt" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 25: / Line 16: @@
 __TOC__
 </SX>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Li, Y]]
+[[Category: Li Y]]
-[[Category: Orth, K]]
+[[Category: Orth K]]
-[[Category: Peng, W]]
+[[Category: Peng W]]
-[[Category: Santos, M de Souza]]
+[[Category: Tomchick DR]]
-[[Category: Tomchick, D R]]
+[[Category: De Souza Santos M]]
-[[Category: Membrane protein]]
-[[Category: Pore-forming toxin]]
-[[Category: Toxin]]

6mrt

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12-meric ClyA pore complex

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