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FEBS Lett. 1999 Sep 24;458(3):429-35.

Binding of calcium in the EF-hand of Escherichia coli lytic transglycosylase Slt35 is important for stability.

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  • 1BIOSON Research Institute and Laboratory of Biophysical Chemistry, University of Groningen, The Netherlands.


The Escherichia coli lytic transglycosylase Slt35 contains a single metal ion-binding site that resembles EF-hand calcium-binding sites. The Slt35 EF-hand is only the second observation of such a domain in a prokaryotic protein. Two crystal structures at 2.1 A resolution show that both Ca2+ ions and Na+ ions can bind to the EF-hand domain, but in subtly different configurations. Heat-induced unfolding studies demonstrate that Ca2+ ions are preferentially bound, and that only Ca2+ ions significantly increase the melting temperature of Slt35. This shows that the EF-hand calcium-binding domain is important for the stability of Slt35.

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