1AGJ

EPIDERMOLYTIC TOXIN A FROM STAPHYLOCOCCUS AUREUS

Summary for 1AGJ

• Entry DOI: 10.2210/pdb1agj/pdb
• Descriptor: EPIDERMOLYTIC TOXIN A (2 entities in total)
• Functional Keywords: hydrolase, serine protease
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 53970.22

Authors

Cavarelli, J. (deposition date: 1997-03-25, release date: 1997-09-26, Last modification date: 2024-02-07)

Primary citation

Cavarelli, J.,Prevost, G.,Bourguet, W.,Moulinier, L.,Chevrier, B.,Delagoutte, B.,Bilwes, A.,Mourey, L.,Rifai, S.,Piemont, Y.,Moras, D.
The structure of Staphylococcus aureus epidermolytic toxin A, an atypic serine protease, at 1.7 A resolution.
Structure, 5:813-824, 1997

PubMed Abstract: Staphylococcal epidermolytic toxins A and B (ETA and ETB) are responsible for the staphylococcal scalded skin syndrome of newborn and young infants; this condition can appear just a few hours after birth. These toxins cause the disorganization and disruption of the region between the stratum spinosum and the stratum granulosum--two of the three cellular layers constituting the epidermis. The physiological substrate of ETA is not known and, consequently, its mode of action in vivo remains an unanswered question. Determination of the structure of ETA and its comparison with other serine proteases may reveal insights into ETA's catalytic mechanism.

PubMed: 9261066
DOI: 10.1016/S0969-2126(97)00235-9

Experimental method

X-RAY DIFFRACTION (1.7 Å)