1EXF

EXFOLIATIVE TOXIN A

Summary for 1EXF

• Entry DOI: 10.2210/pdb1exf/pdb
• Descriptor: EXFOLIATVE TOXIN A, GLYCINE (3 entities in total)
• Functional Keywords: complex (toxin-peptide), hydrolase, serine protease, superantigen, complex (toxin-peptide) complex, complex (toxin/peptide)
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 27060.18

Authors

Vath, G.M.,Earhart, C.A.,Rago, J.V.,Kim, M.H.,Bohach, G.A.,Schlievert, P.M.,Ohlendorf, D.H. (deposition date: 1996-10-22, release date: 1998-02-25, Last modification date: 2024-03-13)

Primary citation

Vath, G.M.,Earhart, C.A.,Rago, J.V.,Kim, M.H.,Bohach, G.A.,Schlievert, P.M.,Ohlendorf, D.H.
The structure of the superantigen exfoliative toxin A suggests a novel regulation as a serine protease.
Biochemistry, 36:1559-1566, 1997

PubMed 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 A 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 alpha 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.

PubMed: 9048539
DOI: 10.1021/bi962614f

Experimental method

X-RAY DIFFRACTION (2.1 Å)