double-psi beta-barrel fold of Streptomyces papain inhibitor and similar proteins
Streptomyces papain inhibitor (SPI) adopts a rigid, thermo-resistant double-psi-beta-barrel (DPBB) fold that is stabilized by two cysteine bridges. SPI serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes, that is used to covalently and specifically link functional amines to glutamine donor sites of therapeutic proteins. SPI is a stress protein produced under hyperthermal stress conditions, and is able to inhibit the cysteine proteases, papain and bromelain, as well as the bovine serine protease trypsin.