Send to

Choose Destination
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.

Author information

BIOSON 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.

[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center