1EWJ

CRYSTAL STRUCTURE OF BLEOMYCIN-BINDING PROTEIN COMPLEXED WITH BLEOMYCIN

1EWJ の概要

• エントリーDOI: 10.2210/pdb1ewj/pdb
• 関連するPDBエントリー: 1BYL 1ECS 1QTO
• 分子名称: BLEOMYCIN RESISTANCE DETERMINANT, BLEOMYCIN A2 (3 entities in total)
• 機能のキーワード: bleomycin-binding protein, bleomycin, antibiotics resistance, homodimer, antibiotic inhibitor
• 由来する生物種: Klebsiella pneumoniae
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 124011.96

構造登録者

Maruyama, M.,Kumagai, T.,Matoba, Y.,Hata, Y.,Sugiyama, M. (登録日: 2000-04-26, 公開日: 2001-04-26, 最終更新日: 2024-02-07)

主引用文献

Maruyama, M.,Kumagai, T.,Matoba, Y.,Hayashida, M.,Fujii, T.,Hata, Y.,Sugiyama, M.
Crystal structures of the transposon Tn5-carried bleomycin resistance determinant uncomplexed and complexed with bleomycin.
J.Biol.Chem., 276:9992-9999, 2001

PubMed Abstract: 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.

PubMed: 11134052
DOI: 10.1074/jbc.M009874200

実験手法

X-RAY DIFFRACTION (2.5 Å)