1QDR

2.1 A RESOLUTION STRUCTURE OF ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35

Summary for 1QDR

• Entry DOI: 10.2210/pdb1qdr/pdb
• Related: 1QUS 1QUT
• Descriptor: LYTIC MUREIN TRANSGLYCOSYLASE B, SODIUM ION, BICINE, ... (5 entities in total)
• Functional Keywords: alpha-helical protein with an five-stranded antiparallel beta-sheet, glycosyl transferase, hydrolase
• Biological source: Escherichia coli
• Cellular location: Cell outer membrane; Lipid-anchor; Periplasmic side: P41052
• Total number of polymer chains: 1
• Total formula weight: 36327.89

Authors

van Asselt, E.J.,Dijkstra, A.J. (deposition date: 1999-07-10, release date: 2000-01-24, Last modification date: 2024-02-14)

Primary citation

van Asselt, E.J.,Dijkstra, B.W.
Binding of calcium in the EF-hand of Escherichia coli lytic transglycosylase Slt35 is important for stability.
FEBS Lett., 458:429-435, 1999

PubMed Abstract: 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.

PubMed: 10570954
DOI: 10.1016/S0014-5793(99)01198-9

Experimental method

X-RAY DIFFRACTION (2.1 Å)