1qdr: Difference between revisions
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[[Image:1qdr.gif|left|200px]] | [[Image:1qdr.gif|left|200px]] | ||
'''2.1 A RESOLUTION STRUCTURE OF ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35''' | {{Structure | ||
|PDB= 1qdr |SIZE=350|CAPTION= <scene name='initialview01'>1qdr</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=BCN:BICINE'>BCN</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''2.1 A RESOLUTION STRUCTURE OF ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1QDR is a [ | 1QDR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QDR OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10570954 10570954] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: glycosyl transferase]] | [[Category: glycosyl transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:36:18 2008'' | ||
Revision as of 11:36, 20 March 2008
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| 1qdr, resolution 2.10Å | |||||||||||||
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| Ligands: | NA, BCN and EDO | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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