1exf

From Proteopedia

Revision as of 14:06, 5 November 2007

EXFOLIATIVE TOXIN A

Overview

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.

About this Structure

1EXF is a Single protein structure of sequence from Staphylococcus aureus and Unidentified with GLY as ligand. Structure known Active Site: CAT. Full crystallographic information is available from OCA.

Reference

The structure of the superantigen exfoliative toxin A suggests a novel regulation as a serine protease., Vath GM, Earhart CA, Rago JV, Kim MH, Bohach GA, Schlievert PM, Ohlendorf DH, Biochemistry. 1997 Feb 18;36(7):1559-66. PMID:9048539

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