Journal article
The Structure of the Superantigen Exfoliative Toxin A Suggests a Novel Regulation as a Serine Protease
Biochemistry (Easton), Vol.36(7), pp.1559-1566
02/18/1997
DOI: 10.1021/bi962614f
PMID: 9048539
Abstract
Exfoliative toxin A (ETA) causes staphylococcal scalded skin syndrome which is characterized by a specific intraepidermal separation of layers of the skin. The mechanism by which ETA causes skin separation is unknown although protease or superantigen activity has been implicated. The X-ray crystal structure of ETA has been solved in two crystal forms to 2.1 and 2.3 Å resolution and R-factors of 17% and 19%, respectively. The structures indicate that ETA belongs to the chymotrypsin-like family of serine proteases and cleaves substrates after acidic residues. The conformation of a loop adjacent to the catalytic site is suggested to be key in regulating the proteolytic activity of ETA through controlling whether the main chain carbonyl group of Pro192 occupies the oxyanion hole. A unique amino-terminal domain containing a 15-residue amphipathic α helix may also be involved in protease activation through binding a specific receptor. Substitution of the active site serine residue with cysteine abolishes the ability of ETA to produce the characteristic separation of epidermal layers but not its ability to induce T cell proliferation.
Details
- Title: Subtitle
- The Structure of the Superantigen Exfoliative Toxin A Suggests a Novel Regulation as a Serine Protease
- Creators
- Gregory M VathCathleen A EarhartJames V RagoMichael H KimGregory A BohachPatrick M SchlievertDouglas H Ohlendorf
- Resource Type
- Journal article
- Publication Details
- Biochemistry (Easton), Vol.36(7), pp.1559-1566
- Publisher
- American Chemical Society
- DOI
- 10.1021/bi962614f
- PMID
- 9048539
- ISSN
- 0006-2960
- eISSN
- 1520-4995
- Language
- English
- Date published
- 02/18/1997
- Academic Unit
- Microbiology and Immunology; Internal Medicine
- Record Identifier
- 9984001218902771
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