Binding of calcium in the EF-hand of Escherichia coli lytic transglycosylase Slt35 is important for stability.
Article Details
- CitationCopy to clipboard
van Asselt EJ, Dijkstra BW
Binding of calcium in the EF-hand of Escherichia coli lytic transglycosylase Slt35 is important for stability.
FEBS Lett. 1999 Sep 24;458(3):429-35.
- PubMed ID
- 10570954 [ View in PubMed]
- Abstract
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.