Tetracycline repressor protein

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{{STRUCTURE_2trt| PDB=2trt | SIZE=400| SCENE= |right|CAPTION=Tetracycline repressor protein complex with tetracycline and Mg+2 ion (green), [[2trt]] }}
{{STRUCTURE_2trt| PDB=2trt | SIZE=400| SCENE= |right|CAPTION=Tetracycline repressor protein complex with tetracycline and Mg+2 ion (green), [[2trt]] }}
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'''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.
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'''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>.
== 3D Structures of tetracycline repressor protein==
== 3D Structures of tetracycline repressor protein==
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:03, 8 September 2016

Template:STRUCTURE 2trt

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].

3D Structures of tetracycline repressor protein

Updated on 08-September-2016

References

  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

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