2XB5

Tet repressor (class D) in complex with 7-Iodotetracycline

Summary for 2XB5

• Entry DOI: 10.2210/pdb2xb5/pdb
• Related: 1A6I 1BJ0 1BJY 1BJZ 1ORK 1QPI 2TCT 2TRT 2VKE 2VKV 2X6O 2X9D
• Descriptor: TETRACYCLINE REPRESSOR PROTEIN CLASS D, 7-IODOTETRACYCLINE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: transcription, antibiotic resistance, metal-binding, transcription regulation
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 23872.40

Authors

Kisker, C.,Saenger, W.,Hinrichs, W. (deposition date: 2010-04-05, release date: 2010-10-06, Last modification date: 2024-05-08)

Primary citation

Hinrichs, W.,Kisker, C.,Duvel, M.,Muller, A.,Tovar, K.,Hillen, W.,Saenger, W.
Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance.
Science, 264:418-420, 1994

PubMed Abstract: 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.

PubMed: 8153629
DOI: 10.1126/science.8153629

Experimental method

X-RAY DIFFRACTION (2.5 Å)