2BDZ

Mexicain from Jacaratia mexicana

Summary for 2BDZ

• Entry DOI: 10.2210/pdb2bdz/pdb
• Related: 1GEC 1MEG 1PCI 1PPO 1YAL
• Descriptor: Mexicain, N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE (3 entities in total)
• Functional Keywords: mexicain, cysteine protease, peptidase_c1, papain-like, hydrolase
• Biological source: Jacaratia mexicana
• Total number of polymer chains: 4
• Total formula weight: 96616.84

Authors

Gavira, J.A.,Oliver-Salvador, M.C.,Gonzalez-Ramirez, L.A.,Soriano-Garcia, M.,Garcia-Ruiz, J.M. (deposition date: 2005-10-21, release date: 2006-10-03, Last modification date: 2025-11-12)

Primary citation

Gavira, J.A.,Gonzalez-Ramirez, L.A.,Oliver-Salvador, M.C.,Soriano-Garcia, M.,Garcia-Ruiz, J.M.
Structure of the mexicain-E-64 complex and comparison with other cysteine proteases of the papain family.
Acta Crystallogr.,Sect.D, 63:555-563, 2007

PubMed 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.

PubMed: 17452780
DOI: 10.1107/S0907444907005616

Experimental method

X-RAY DIFFRACTION (2.1 Å)