Protein Family Models

Staphostatin B inhibits the cysteine protease Staphopain B, produced by Staphylococcus aureus, by blocking the active site of the enzyme. The domain adopts an eight-stranded mixed beta-barrel structure, with a deviation from the up-down topology of canonical beta-barrels in the amino-terminal part of the molecule [1]. [1]. 15644332. A comparison of staphostatin B with standard mechanism serine. protease inhibitors.. Filipek R, Potempa J, Bochtler M;. J Biol Chem. 2005;280:14669-14674. (from Pfam)

Date:

2024-08-14

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)

Date:

2024-08-14

Staphostatin B is an endogenous inhibitor of staphopains, the major cysteine proteases secreted by Staphylococcus aureus.

Gene:

sspC

Date:

2019-09-18