1qdr
From Proteopedia
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|PDB= 1qdr |SIZE=350|CAPTION= <scene name='initialview01'>1qdr</scene>, resolution 2.10Å | |PDB= 1qdr |SIZE=350|CAPTION= <scene name='initialview01'>1qdr</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BCN:BICINE'>BCN</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1qus|1QUS]], [[1qut|1QUT]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qdr OCA], [http://www.ebi.ac.uk/pdbsum/1qdr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qdr RCSB]</span> | ||
}} | }} | ||
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[[Category: Asselt, E J.van.]] | [[Category: Asselt, E J.van.]] | ||
[[Category: Dijkstra, A J.]] | [[Category: Dijkstra, A J.]] | ||
| - | [[Category: BCN]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: NA]] | ||
[[Category: alpha-helical protein with an five-stranded antiparallel beta-sheet]] | [[Category: alpha-helical protein with an five-stranded antiparallel beta-sheet]] | ||
[[Category: glycosyl transferase]] | [[Category: glycosyl transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:12:18 2008'' |
Revision as of 20:12, 30 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1QUS, 1QUT
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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