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]] }}
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{{STRUCTURE_2trt| PDB=2trt | SIZE=350| SCENE= |right|CAPTION=Tetracycline repressor protein complex with tetracycline and Mg+2 ion (green), [[2trt]] }}
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== 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>.
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== Structural highlights ==
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TetR binds DNA with a helix-turn-helix motif. The inhibitor TC binds in the active site to several TetR side chains and to an octahedrally-coordinated Mg+2 ion<ref>PMID:8153629</ref>.
== 3D Structures of tetracycline repressor protein==
== 3D Structures of tetracycline repressor protein==

Revision as of 09:32, 8 September 2016

Template:STRUCTURE 2trt

Contents

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].

Structural highlights

TetR binds DNA with a helix-turn-helix motif. The inhibitor TC binds in the active site to several TetR side chains and to an octahedrally-coordinated Mg+2 ion[2].

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
  2. ↑ 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

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