Tetracycline repressor protein
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
<StructureSection load='2trt' size='350' side='right' scene='47/477771/Cv/1' caption='Tetracycline repressor protein complex with tetracycline and Mg+2 ion (green), [[2trt]]'> | <StructureSection load='2trt' size='350' side='right' scene='47/477771/Cv/1' caption='Tetracycline repressor protein complex with tetracycline and Mg+2 ion (green), [[2trt]]'> | ||
== Function == | == 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<ref>PMID:21261817</ref>. | + | '''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<ref>PMID:21261817</ref>. '''HTH-type TetR''' is a prokaryotic TetR which contains a DNA-binding '''H'''elix-'''T'''urn-'''H'''elix domain of ca. 60 residues. |
== Structural highlights == | == Structural highlights == | ||
Revision as of 10:25, 24 November 2020
| |||||||||||
References
- ↑ 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
- ↑ 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
