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Structure of the mexicain-E-64 complex and comparison with other cysteine proteases of the papain family

AutorGavira Gallardo, J. A. ; González-Ramírez, L. A.; Oliver-Salvador, M. C.; Soriano-García, M.; García Ruiz, Juan Manuel
Palabras claveMexicain
Cysteine proteases
Fecha de publicaciónmay-2007
EditorInternational Union of Crystallography
CitaciónActa Crystallographica Section D 63(5): 555-563 (2007)
ResumenMexicain 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 Å resolution and refined to an R factor of 17.7% (Rfree = 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.
Descripción9 pages, 4 tables, 5 figures.
Versión del editorhttp://dx.doi.org/10.1107/S0907444907005616
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