FEBS Letters | |
Binding of calcium in the EF‐hand of Escherichia coli lytic transglycosylase Slt35 is important for stability | |
Dijkstra, Bauke W1  van Asselt, Erik J1  | |
[1] BIOSON Research Institute and Laboratory of Biophysical Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands | |
关键词: EF-hand; Lytic transglycosylase; Thermostability; Crystal structure; Calcium; Escherichia coli; | |
DOI : 10.1016/S0014-5793(99)01198-9 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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 Å 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.
【 授权许可】
Unknown
【 预 览 】
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