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Updated: May 2, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
Published on: January 10, 2018
Crystal structure analysis of EstA from Arthrobacter sp. Rue61a--an insight into catalytic promiscuity
Ulrike Gabriella Wagner1, Frank DiMaio2, Stephan Kolkenbrock3
1Institute of Molecular Biosciences, University of Graz, A-8010 Graz, Austria.
Abstract:
In this article we analyze the reasons for catalytic promiscuity of a type VIII esterase with β-lactamase fold and the ability to cleave β-lactams. We compared the structure of this enzyme to those of an esterase of the same type without any lactamase ability, an esterase with moderate lactamase ability, and a class C β-lactamase with similar fold. Our results show that for these enzymes, the difference in the substrate specificity is sterically driven.
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