1qdr: Difference between revisions

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[[Image:1qdr.gif|left|200px]]
{{Seed}}
[[Image:1qdr.png|left|200px]]


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{{STRUCTURE_1qdr|  PDB=1qdr  |  SCENE=  }}  
{{STRUCTURE_1qdr|  PDB=1qdr  |  SCENE=  }}  


'''2.1 A RESOLUTION STRUCTURE OF ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35'''
===2.1 A RESOLUTION STRUCTURE OF ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35===




==Overview==
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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.
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{{ABSTRACT_PUBMED_10570954}}


==About this Structure==
==About this Structure==
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[[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]]
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Revision as of 10:52, 29 July 2008

File:1qdr.png

Template:STRUCTURE 1qdr

2.1 A RESOLUTION STRUCTURE OF ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35

Template:ABSTRACT PUBMED 10570954

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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