Tetracycline repressor protein

Function

Tetracycline repressor protein (TetR) causes the resistance of bacterial cells to antibiotics like tetracycline (TC). TetR binds TC with higher affinity than the ribosome thus preventing TC from binding there and inhibiting the pathogenic bacteria protein synthesis^[1]. HTH-type TetR is a prokaryotic TetR which contains a DNA-binding Helix-Turn-Helix domain of ca. 60 residues^[2].

Structural highlights

TetR binds DNA with a helix-turn-helix motif. The ^[3]. Water molecules are shown as red spheres. .

3D Structures of tetracycline repressor protein

Tetracycline repressor protein 3D structures

Tetracycline repressor protein complex with tetracycline and Mg+2 ion (green), 2trt

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Bertram R, Hillen W. The application of Tet repressor in prokaryotic gene regulation and expression. Microb Biotechnol. 2008 Jan;1(1):2-16. doi: 10.1111/j.1751-7915.2007.00001.x. PMID:21261817 doi:http://dx.doi.org/10.1111/j.1751-7915.2007.00001.x
↑ Aramaki H, Yagi N, Suzuki M. Residues important for the function of a multihelical DNA binding domain in the new transcription factor family of Cam and Tet repressors. Protein Eng. 1995 Dec;8(12):1259-66. doi: 10.1093/protein/8.12.1259. PMID:8869638 doi:http://dx.doi.org/10.1093/protein/8.12.1259
↑ 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. 1994 Apr 15;264(5157):418-20. PMID:8153629

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Michal Harel, Alexander Berchansky

[1] Bertram R, Hillen W. The application of Tet repressor in prokaryotic gene regulation and expression. Microb Biotechnol. 2008 Jan;1(1):2-16. doi: 10.1111/j.1751-7915.2007.00001.x. PMID:21261817 doi:http://dx.doi.org/10.1111/j.1751-7915.2007.00001.x

[2] Aramaki H, Yagi N, Suzuki M. Residues important for the function of a multihelical DNA binding domain in the new transcription factor family of Cam and Tet repressors. Protein Eng. 1995 Dec;8(12):1259-66. doi: 10.1093/protein/8.12.1259. PMID:8869638 doi:http://dx.doi.org/10.1093/protein/8.12.1259

[3] 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. 1994 Apr 15;264(5157):418-20. PMID:8153629

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