1qdr
From Proteopedia
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'''2.1 A RESOLUTION STRUCTURE OF ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35''' | '''2.1 A RESOLUTION STRUCTURE OF ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35''' | ||
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[[Category: Asselt, E J.van.]] | [[Category: Asselt, E J.van.]] | ||
[[Category: Dijkstra, A J.]] | [[Category: Dijkstra, A J.]] | ||
| - | [[Category: | + | [[Category: Alpha-helical protein with an five-stranded antiparallel beta-sheet]] |
| - | [[Category: | + | [[Category: Glycosyl transferase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:10:11 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:10, 3 May 2008
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 Page seeded by OCA on Sat May 3 06:10:11 2008
