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staphostatin A
The staphostatin A polypeptide chain folds into a slightly deformed, eight-stranded beta-barrel, with strands beta-4 through beta-8 forming an antiparallel sheet while the N-terminus forms a a psi-loop motif. Members of this family constitute a class of cysteine protease inhibitors distinct in the fold and the mechanism of action from any known inhibitors of these enzymes [1]. [1]. 14621990. A novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureus. Dubin G, Krajewski M, Popowicz G, Stec-Niemczyk J, Bochtler M, Potempa J, Dubin A, Holak TA;. Biochemistry. 2003;42:13449-13456. (from Pfam)
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