1LSP

THE CRYSTAL STRUCTURE OF A BULGECIN-INHIBITED G-TYPE LYSOZYME FROM THE EGG-WHITE OF THE AUSTRALIAN BLACK SWAN. A COMPARISON OF THE BINDING OF BULGECIN TO THREE MURAMIDASES

Summary for 1LSP

• Entry DOI: 10.2210/pdb1lsp/pdb
• Descriptor: LYSOZYME, BULGECIN A (3 entities in total)
• Functional Keywords: hydrolase (o-glycosyl)
• Biological source: Cygnus atratus (black swan)
• Cellular location: Secreted: P00717
• Total number of polymer chains: 1
• Total formula weight: 20985.72

Authors

Karlsen, S.,Rao, Z.H.,Hough, E.,Isaacs, N.W. (deposition date: 1995-02-09, release date: 1996-01-01, Last modification date: 2024-10-23)

Primary citation

Karlsen, S.,Hough, E.,Rao, Z.H.,Isaacs, N.W.
Structure of a bulgecin-inhibited g-type lysozyme from the egg white of the Australian black swan. A comparison of the binding of bulgecin to three muramidases.
Acta Crystallogr.,Sect.D, 52:105-114, 1996

PubMed Abstract: Bulgecin A, a bacterial metabolite, has been shown to bind in the active-site groove of the chicken-type lysozyme from the rainbow trout (RBTL) and in the lysozyme-like C-terminal domain, of a soluble lytic transglycosylase (C-SLT) from Escherichia coli. These enzymes are muramidases that cleave the glycosidic bonds in the glycan strands of the murein polymer. Here we report the crystal structure of a complex between the goose-type lysozyme from the egg white of the Australian black swan (SEWL) and bulgecin A at 2.45 A resolution. As is the case for the C-SLT/bulgecin and RBTL/bulgecin complexes, the ligand binds with the N-acetylglucosamine ring in subsite C and the proline moiety in site D where it interacts with the catalytic glutamic acid. The taurine residue interacts with the beta-sheet region. Comparisons of the three buigecin complexes show that the inhibitor has the same binding mode to the muramidases with similar protein-ligand interactions, particularly for SEWL and RBTL. From our results, it seems likely that bulgecin, in general, inhibits enzymes with lysozyme-like domains and thus might represent a novel class of natural antibiotics that act on murein-degrading rather than murein-synthesizing enzymes.

PubMed: 15299731
DOI: 10.1107/S0907444995008468

Experimental method

X-RAY DIFFRACTION (2.45 Å)