tailieunhanh - Báo cáo khoa học: Structural insights into the substrate specificity and activity of ervatamins, the papain-like cysteine proteases from a tropical plant, Ervatamia coronaria

Multiple proteases of the same family are quite often present in the same species in biological systems. These multiple proteases, despite having high homology in their primary and tertiary structures, show deviations in prop-erties such as stability, activity, and specificity. | ỊFEBS Journal Structural insights into the substrate specificity and activity of ervatamins the papain-like cysteine proteases from a tropical plant Ervatamia coronaria Raka Ghosh Sibani Chakraborty Chandana Chakrabarti Jiban Kanti Dattagupta and Sampa Biswas Crystallography and Molecular Biology Division Saha Institute of Nuclear Physics Kolkata India Keywords 3D structures inhibitor complexes multiple enzymes plant cysteine proteases proteolytic activity Correspondence J. K. Dattagupta Crystallography and Molecular Biology Division Saha Institute of Nuclear Physics 1 AF Bidhannagar Kolkata 700 064 India Fax 91 33 23374637 Tel 91 33 23214986 Email Database The cDNA sequence of ervatamin-A has been deposited in the NCBI GenBank with accession number EF591130. The coordinates and structure factors have been deposited in the Protein Data Bank with accession codes 3BCN and 2PRE for the two crystal structures ervatamin-A and erva-tamin-C both complexed with E-64 Received 25 August 2007 revised 16 November 2007 accepted 27 November 2007 doi Multiple proteases of the same family are quite often present in the same species in biological systems. These multiple proteases despite having high homology in their primary and tertiary structures show deviations in properties such as stability activity and specificity. It is of interest therefore to compare the structures of these multiple proteases in a single species to identify the structural changes if any that may be responsible for such deviations. Ervatamin-A ervatamin-B and ervatamin-C are three such papain-like cysteine proteases found in the latex of the tropical plant Erva-tamia coronaria and are known not only for their high stability over a wide range of temperature and pH but also for variations in activity and specificity among themselves and among other members of the family. Here we report the crystal structures of ervatamin-A and ervatamin-C complexed

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