1qdr
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(New page: 200px<br /><applet load="1qdr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qdr, resolution 2.10Å" /> '''2.1 A RESOLUTION STR...)
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Revision as of 22:29, 20 November 2007
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2.1 A RESOLUTION STRUCTURE OF ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35
Overview
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.
About this Structure
1QDR is a Single protein structure of sequence from Escherichia coli with NA, BCN and EDO as ligands. Full crystallographic information is available from OCA.
Reference
Binding of calcium in the EF-hand of Escherichia coli lytic transglycosylase Slt35 is important for stability., van Asselt EJ, Dijkstra BW, FEBS Lett. 1999 Sep 24;458(3):429-35. PMID:10570954
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