S. Karlsen et E. Hough, STRUCTURE OF A COMPLEX BETWEEN BULGECIN, A BACTERIAL METABOLITE, AND LYSOZYME FROM THE RAINBOW-TROUT, Acta crystallographica. Section D, Biological crystallography, 52, 1996, pp. 115-123
Citations number
36
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
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-lacta
m antibiotics. The compound does not itself exhibit any antibacterial
activity, but has been shown to inhibit a soluble lyric transglycosyla
se (SLT70) from Escherichia coil which has a lysozyme-like domain. Rec
ently, the crystal structure of an SLT-bulgecin complex has been deter
mined to 3.5 Angstrom resolution. We report here the crystal structure
of a complex between lysozyme from the rainbow trout (RBTL) and bulge
cin A at 2.0 Angstrom resolution. As for the SLT-bulgecin complex, bul
gecin is bound with the glycosaminyl moiety in subsite C and the proli
ne 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 par
t of the active-site cleft. From the observed position of the bulgecin
molecule, it seems reasonable that it is an inhibitor of rainbow trou
t lysozyme. The lysozymes may, in general, be a target for the design
of a novel type of antibiotics distinct from the beta-lactams which ar
e insensitive to the muramidases.