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2XB5

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

Summary for 2XB5
Entry DOI10.2210/pdb2xb5/pdb
Related1A6I 1BJ0 1BJY 1BJZ 1ORK 1QPI 2TCT 2TRT 2VKE 2VKV 2X6O 2X9D
DescriptorTETRACYCLINE REPRESSOR PROTEIN CLASS D, 7-IODOTETRACYCLINE, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordstranscription, antibiotic resistance, metal-binding, transcription regulation
Biological source Escherichia coli
Total number of polymer chains1
Total formula weight23872.40
Authors
Kisker, C.,Saenger, W.,Hinrichs, W. (deposition date: 2010-04-05, release date: 2010-10-06, Last modification date: 2024-05-08)
Primary citationHinrichs, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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