PDBsum entry 1lmu

Isomerase

PDB id: 1lmu

Contents

Protein chain

649 a.a.

Theoretical model

PDB id:

1lmu

Name:

Isomerase

Title:

Structure of DNA topoisomerase iii-salmonella typhimurium

Structure:

DNA topoisomerase iii. Chain: a. Ec: 5.99.1.2

Source:

Salmonella typhimurium. Bacteria

Authors:

R.Sagajkar

Key ref:

S.Karlsen and E.Hough (1996). Structure of a complex between bulgecin, a bacterial metabolite, and lysozyme from the rainbow trout. Acta Crystallogr D Biol Crystallogr, 52, 115-123. PubMed id: 15299732 DOI: 10.1107/S0907444995006366

Date:

02-May-02 Release date: 05-Jun-02

Protein chain

P40687  (TOP3_SALTY) -  DNA topoisomerase 3

Seq: 649 a.a.

Struc: 649 a.a.

DOI no: 10.1107/S0907444995006366

Acta Crystallogr D Biol Crystallogr 52:115-123 (1996)

PubMed id: 15299732

Structure of a complex between bulgecin, a bacterial metabolite, and lysozyme from the rainbow trout.

S.Karlsen, E.Hough.

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.

Selected figure(s)

Figure 3.
Fig. 3. Observed electron density ([Fo[- IFcl omit map), contoured at 0.12 e A -3 for bulgecin bound in the active-site cleft of RBTL. Bulgecin was omitted from the coordinate file.

Figure 6.
Fig. 6. Hydrogen-bonding inter- actios between RBTL and bulgein. The lysozyme strucure is shown with thin lines, bulgecn with thick lines and hydrogen bonds with broken lines. Water molecules are depicted with crosses.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1996, 52, 115-123) copyright 1996.

Figures were selected by an automated process.