1qdr: Difference between revisions

Revision as of 15:38, 21 February 2008

2.1 A RESOLUTION STRUCTURE OF ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35

OverviewOverview

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 StructureAbout this Structure

1QDR is a Single protein structure of sequence from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 14:38:33 2008

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OCA

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-[[Image:1qdr.gif|left|200px]]<br /><applet load="1qdr" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1qdr.gif|left|200px]]<br /><applet load="1qdr" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1qdr, resolution 2.10&Aring;" />
 '''2.1 A RESOLUTION STRUCTURE OF ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35'''<br />
 ==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.
+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==
-QDR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with NA, BCN and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QDR OCA].
+QDR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=BCN:'>BCN</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QDR OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Asselt, E.J.van.]]
+[[Category: Asselt, E J.van.]]
-[[Category: Dijkstra, A.J.]]
+[[Category: Dijkstra, A J.]]
 [[Category: BCN]]
 [[Category: EDO]]
@@ Line 21: / Line 21: @@
 [[Category: glycosyl transferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:36:25 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:33 2008''