1LMC

THE CRYSTAL STRUCTURE OF A COMPLEX BETWEEN BULGECIN, A BACTERIAL METABOLITE, AND LYSOZYME FROM THE RAINBOW TROUT

Summary for 1LMC

• Entry DOI: 10.2210/pdb1lmc/pdb
• Descriptor: LYSOZYME, BULGECIN A (3 entities in total)
• Functional Keywords: hydrolase (o-glycosyl)
• Biological source: Oncorhynchus mykiss (rainbow trout)
• Cellular location: Secreted: P11941
• Total number of polymer chains: 1
• Total formula weight: 14854.61

Authors

Karlsen, S.,Hough, E. (deposition date: 1994-11-14, release date: 1996-01-01, Last modification date: 2024-10-30)

Primary citation

Karlsen, S.,Hough, E.
Structure of a complex between bulgecin, a bacterial metabolite, and lysozyme from the rainbow trout.
Acta Crystallogr.,Sect.D, 52:115-123, 1996

PubMed Abstract: Bulgecin, a sulfonated glycopeptide produced by Pseudomonas acidophila and Pseudomonas mesoacidophila, induces bulge formation and enhances lysis of bacterial cell walls when used in combination with beta-lactam antibiotics. The compound does not itself exhibit any antibacterial activity, but has been shown to inhibit a soluble lytic transglycosylase (SLT70) from Escherichia coli which has a lysozyme-like domain. Recently, the crystal structure of an SLT-bulgecin complex has been determined to 3.5 A resolution. We report here the crystal structure of a complex between lysozyme from the rainbow trout (RBTL) and bulgecin A at 2.0 A resolution. As for the SLT-bulgecin complex, bulgecin is bound with the glycosaminyl moiety in subsite C and the proline residue in site D of the active-site cleft of RBTL, where it makes hydrogen-bonding interactions with the catalytic residues. The taurine moiety is bound to the left side of subsites E and F in the lower part of the active-site cleft. From the observed position of the bulgecin molecule, it seems reasonable that it is an inhibitor of rainbow trout lysozyme. The lysozymes may, in general, be a target for the design of a novel type of antibiotics distinct from the beta-lactams which are insensitive to the muramidases.

PubMed: 15299732
DOI: 10.1107/S0907444995006366

Experimental method

X-RAY DIFFRACTION (2 Å)