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| | <StructureSection load='4p1y' size='340' side='right'caption='[[4p1y]], [[Resolution|resolution]] 2.99Å' scene=''> | | <StructureSection load='4p1y' size='340' side='right'caption='[[4p1y]], [[Resolution|resolution]] 2.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4p1y]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Staam Staam]. 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 with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_Mu50 Staphylococcus aureus subsp. aureus Mu50]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4P1Y FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p1x|4p1x]], [[4p24|4p24]]</td></tr> | + | </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=4p1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p1y OCA], [https://pdbe.org/4p1y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p1y RCSB], [https://www.ebi.ac.uk/pdbsum/4p1y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p1y ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hlgB, SAV2421 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158878 STAAM]), hlgA, hlg2, SAV2419 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158878 STAAM])</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://pdbe.org/4p1y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p1y RCSB], [http://www.ebi.ac.uk/pdbsum/4p1y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p1y ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HLGA_STAAM HLGA_STAAM]] Toxin that seems to act by forming pores in the membrane of the cell. Has a hemolytic and a leucotoxic activity (By similarity). | + | [https://www.uniprot.org/uniprot/A0A0H3JX61_STAAM A0A0H3JX61_STAAM] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Hemolysin|Hemolysin]] | + | *[[Hemolysin 3D structures|Hemolysin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Staam]] | + | [[Category: Staphylococcus aureus subsp. aureus Mu50]] |
| - | [[Category: Tanaka, I]] | + | [[Category: Tanaka I]] |
| - | [[Category: Tanaka, Y]] | + | [[Category: Tanaka Y]] |
| - | [[Category: Yamashita, D]] | + | [[Category: Yamashita D]] |
| - | [[Category: Yao, M]] | + | [[Category: Yao M]] |
| - | [[Category: Pore forming toxin]]
| + | |
| - | [[Category: Toxin]]
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| Structural highlights
Function
A0A0H3JX61_STAAM
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yamashita D, Sugawara T, Takeshita M, Kaneko J, Kamio Y, Tanaka I, Tanaka Y, Yao M. Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins. Nat Commun. 2014 Sep 29;5:4897. doi: 10.1038/ncomms5897. PMID:25263813 doi:http://dx.doi.org/10.1038/ncomms5897
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