1ecs

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1ecs, resolution 1.70Å

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THE 1.7 A CRYSTAL STRUCTURE OF A BLEOMYCIN RESISTANCE DETERMINANT ENCODED ON THE TRANSPOSON TN5

Overview

The transposon Tn5 carries a gene designated ble that confers resistance, to bleomycin (Bm). In this study, we determined the x-ray crystal, structures of the ble gene product, designated BLMT, uncomplexed and, complexed with Bm at 1.7 and 2.5 A resolution, respectively. The structure, of BLMT is a dimer with two Bm-binding pockets composed of two large, concavities and two long grooves. This crystal structure of BLMT complexed, with Bm gives a precise mode for binding of the antibiotic to BLMT. The, conformational change of BLMT generated by binding to Bm occurs at a, beta-turn composed of the residues from Gln(97) to Thr(102)., Crystallographic analysis of Bm bound to BLMT shows that two thiazolium, rings of the bithiazole moiety are in the trans conformation. The axial, ligand, which binds a metal ion, seems to be the primary amine in the, beta-aminoalanine moiety. This report, which is the first with regard to, the x-ray crystal structure of Bm, shows that the bithiazole moiety of Bm, is far from the metal-binding domain. That is, Bm complexed with BLMT, takes a more extended form than the drug complexed with DNA.

About this Structure

1ECS is a Single protein structure of sequence from Klebsiella pneumoniae with CA and PG4 as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structures of the transposon Tn5-carried bleomycin resistance determinant uncomplexed and complexed with bleomycin., Maruyama M, Kumagai T, Matoba Y, Hayashida M, Fujii T, Hata Y, Sugiyama M, J Biol Chem. 2001 Mar 30;276(13):9992-9. Epub 2000 Dec 29. PMID:11134052

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