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- W1970179681 abstract "Mexicain is a 23.8 kDa cysteine protease from the tropical plant Jacaratia mexicana. It is isolated as the most abundant product after cation-exchange chromatography of the mix of proteases extracted from the latex of the fruit. The purified enzyme inhibited with E-64 [N-(3-carboxyoxirane-2-carbonyl)-leucyl-amino(4-guanido)butane] was crystallized by sitting-drop vapour diffusion and the structure was solved by molecular replacement at 2.1 A resolution and refined to an R factor of 17.7% (R(free) = 23.8%). The enzyme belongs to the alpha+beta class of proteins and the structure shows the typical papain-like fold composed of two domains, the alpha-helix-rich (L) domain and the beta-barrel-like (R) domain, separated by a groove containing the active site formed by residues Cys25 and His159, one from each domain. The four monomers in the asymmetric unit show one E-64 molecule covalently bound to Cys25 in the active site and differences have been found in the placement of E-64 in each monomer." @default.
- W1970179681 created "2016-06-24" @default.
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- W1970179681 date "2007-04-21" @default.
- W1970179681 modified "2023-10-18" @default.
- W1970179681 title "Structure of the mexicain–E-64 complex and comparison with other cysteine proteases of the papain family" @default.
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- W1970179681 doi "https://doi.org/10.1107/s0907444907005616" @default.
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