1d0l
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(New page: 200px<br /><applet load="1d0l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d0l, resolution 1.97Å" /> '''THE ESCHERICHIA COLI...)
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Revision as of 10:47, 20 November 2007
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THE ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35 IN COMPLEX WITH BULGECIN A
Overview
Lytic transglycosylases catalyze the cleavage of the beta-1, 4-glycosidic, bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine, (GlcNAc) in peptidoglycan with concomitant formation of a 1,6-anhydro bond, in the MurNAc residue. To understand the reaction mechanism of Escherichia, coli lytic transglycosylase Slt35, three crystal structures have been, determined of Slt35 in complex with two different peptidoglycan fragments, and with the lytic transglycosylase inhibitor bulgecin A. The complexes, define four sugar-binding subsites (-2, -1, +1, and +2) and two, peptide-binding sites in a large cleft close to Glu162. The Glu162 side, chain is between the -1 and +1 sugar-binding sites, in agreement with a, function as catalytic acid/base. The complexes suggest additional, contributions to catalysis from Ser216 and Asn339, residues which are, conserved among the MltB/Slt35 lytic transglycosylases.
About this Structure
1D0L is a Single protein structure of sequence from Escherichia coli with CA and BLG as ligands. Full crystallographic information is available from OCA.
Reference
Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan., van Asselt EJ, Kalk KH, Dijkstra BW, Biochemistry. 2000 Feb 29;39(8):1924-34. PMID:10684641
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