Na+/K+ exchange switches the catalytic apparatus of K-dependent plant L-asparaginase.

Bejger, M., Imiolczyk, B., Clavel, D., Gilski, M., Pajak, A., Marsolais, F., and Jaskolski, M. (2014). "Na+/K+ exchange switches the catalytic apparatus of K-dependent plant L-asparaginase.", Acta Crystallographica Section D Biological Crystallography, 70(7), pp. 1854-1872. doi : 10.1107/s1399004714008700  Access to full text

Abstract

Three crystal structures of potassium-dependent plant L-asparaginase were solved in complexes with K+, Na+, and both cations. A novel alkali metal binding loop Val111-Ser118 (the activation loop) changes its conformation upon K+/Na+ exchange, leading to a reconfiguration of three key residues, His117, Arg224, Glu250 (the catalytic switch), to allow or prevent substrate binding in the active site of the enzyme.

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