1D0K
THE ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35 IN COMPLEX WITH TWO MURODIPEPTIDES (GLCNAC-MURNAC-L-ALA-D-GLU)
Summary for 1D0K
| Entry DOI | 10.2210/pdb1d0k/pdb |
| Related | 1D0K 1D0L 1D0M 1QDR 1QDT 1QUS 1QUT |
| Descriptor | 35KD SOLUBLE LYTIC TRANSGLYCOSYLASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-N-acetyl-beta-muramic acid, CALCIUM ION, ... (7 entities in total) |
| Functional Keywords | alpha-helical protein with a five-stranded antiparallel beta-sheet, glycosyltransferase, ef-hand, transferase |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane; Lipid-anchor; Periplasmic side: P41052 |
| Total number of polymer chains | 1 |
| Total formula weight | 37677.20 |
| Authors | van Asselt, E.J.,Kalk, K.H.,Dijkstra, B.W. (deposition date: 1999-09-12, release date: 2000-03-06, Last modification date: 2024-02-07) |
| Primary citation | van Asselt, E.J.,Kalk, K.H.,Dijkstra, B.W. Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan. Biochemistry, 39:1924-1934, 2000 Cited by PubMed Abstract: 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. PubMed: 10684641DOI: 10.1021/bi992161p PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.02 Å) |
Structure validation
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