Publication Date:
1996-12-13
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Song, L -- Hobaugh, M R -- Shustak, C -- Cheley, S -- Bayley, H -- Gouaux, J E -- New York, N.Y. -- Science. 1996 Dec 13;274(5294):1859-66.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Chicago, 920 East 58 Street, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8943190" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Bacterial Toxins/*chemistry/metabolism
;
Cell Membrane/chemistry/metabolism
;
Crystallography, X-Ray
;
Hemolysin Proteins/*chemistry/metabolism
;
Hydrogen Bonding
;
Lipid Bilayers/*chemistry
;
Membrane Potentials
;
Models, Molecular
;
Molecular Sequence Data
;
*Protein Conformation
;
Protein Folding
;
Protein Structure, Secondary
;
Staphylococcus aureus/*chemistry
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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