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4p1y
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4p1y]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P1Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P1Y FirstGlance]. <br> | <table><tr><td colspan='2'>[[4p1y]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P1Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P1Y FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p1x|4p1x]], [[4p24|4p24]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p1x|4p1x]], [[4p24|4p24]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4p1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p1y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p1y RCSB], [http://www.ebi.ac.uk/pdbsum/4p1y PDBsum]</span></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=4p1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p1y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p1y RCSB], [http://www.ebi.ac.uk/pdbsum/4p1y PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pathogenic bacteria secrete pore-forming toxins (PFTs) to attack target cells. PFTs are expressed as water-soluble monomeric proteins, which oligomerize into nonlytic prepore intermediates on the target cell membrane before forming membrane-spanning pores. Despite a wealth of biochemical data, the lack of high-resolution prepore structural information has hampered understanding of the beta-barrel formation process. Here, we report crystal structures of staphylococcal gamma-haemolysin and leucocidin prepores. The structures reveal a disordered bottom half of the beta-barrel corresponding to the transmembrane region, and a rigid upper extramembrane half. Spectroscopic analysis of fluorescently labelled mutants confirmed that the prepore is distinct from the pore within the transmembrane region. Mutational analysis also indicates a pivotal role for the glycine residue located at the lipid-solvent interface as a 'joint' between the two halves of the beta-barrel. These observations suggest a two-step transmembrane beta-barrel pore formation mechanism in which the upper extramembrane and bottom transmembrane regions are formed independently. | ||
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| + | Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins.,Yamashita D, Sugawara T, Takeshita M, Kaneko J, Kamio Y, Tanaka I, Tanaka Y, Yao M Nat Commun. 2014 Sep 29;5:4897. doi: 10.1038/ncomms5897. PMID:25263813<ref>PMID:25263813</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:30, 20 October 2014
Crystal structure of staphylococcal gamma-hemolysin prepore
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