7ahl

<StructureSection load='7ahl' size='340' side='right' caption='[[7ahl]], [[Resolution|resolution]] 1.89&Aring;' scene=''>

<table><tr><td colspan='2'>[[7ahl]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=7AHL FirstGlance]. <br>

</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=7ahl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ahl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=7ahl RCSB], [http://www.ebi.ac.uk/pdbsum/7ahl PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/HLA_STAAU HLA_STAAU]] Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Heptamer oligomerization and pore formation is required for lytic activity.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ah/7ahl_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

The structure of the Staphylococcus aureus alpha-hemolysin pore has been determined to 1.9 A resolution. Contained within the mushroom-shaped homo-oligomeric heptamer is a solvent-filled channel, 100 A in length, that runs along the sevenfold axis and ranges from 14 A to 46 A in diameter. The lytic, transmembrane domain comprises the lower half of a 14-strand antiparallel beta barrel, to which each protomer contributes two beta strands, each 65 A long. The interior of the beta barrel is primarily hydrophilic, and the exterior has a hydrophobic belt 28 A wide. The structure proves the heptameric subunit stoichiometry of the alpha-hemolysin oligomer, shows that a glycine-rich and solvent-exposed region of a water-soluble protein can self-assemble to form a transmembrane pore of defined structure, and provides insight into the principles of membrane interaction and transport activity of beta barrel pore-forming toxins.

Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore.,Song L, Hobaugh MR, Shustak C, Cheley S, Bayley H, Gouaux JE Science. 1996 Dec 13;274(5294):1859-66. PMID:8943190<ref>PMID:8943190</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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*[[User:Eric Martz/JSmol Notes|User:Eric Martz/JSmol Notes]]

== References ==

<references/>

[[Category: Bayley, H]]

[[Category: Cheley, S]]

[[Category: Gouaux, J E]]

[[Category: Hobaugh, M]]

[[Category: Shustak, C]]

[[Category: Song, L]]

[[Category: Transmembrane pore]]