STRUCTURE OF THE TET REPRESSOR TETRACYCLINE COMPLEX AND REGULATION OF ANTIBIOTIC-RESISTANCE

被引:344
作者
HINRICHS, W [1 ]
KISKER, C [1 ]
DUVEL, M [1 ]
MULLER, A [1 ]
TOVAR, K [1 ]
HILLEN, W [1 ]
SAENGER, W [1 ]
机构
[1] UNIV ERLANGEN NURNBERG,INST MIKROBIOL & BIOCHEM,D-91058 ERLANGEN,GERMANY
关键词
D O I
10.1126/science.8153629
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The most frequently occurring resistance of Gram-negative bacteria against tetracyclines is triggered by drug recognition of the Tet repressor. This causes dissociation of the repressor-operator DNA complex and enables expression of the resistance protein TetA, which is responsible for active efflux of tetracycline. The 2.5 angstrom resolution crystal structure of the homodimeric Tet repressor complexed with tetracycline-magnesium reveals detailed drug recognition. The orientation of the operator-binding helix-turn-helix motifs of the repressor is inverted in comparison with other DNA binding proteins. The repressor-drug complex is unable to interact with DNA because the separation of the DNA binding motifs is 5 angstroms wider than usually observed.
引用
收藏
页码:418 / 420
页数:3
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