Tetracycline repressor protein

(Difference between revisions)

Revision as of 12:56, 19 September 2019

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

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Updated on 19-September-2019

↑ 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

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 == Structural highlights ==
-TetR binds DNA with a helix-turn-helix motif.  The <scene name='47/477771/Cv/2'>inhibitor TC binds in the active site to several TetR side chains and to an octahedraly-coordinated Mg+2 ion</scene> <ref>PMID:8153629</ref>. Water molecules shown as red spheres. <scene name='47/477771/Cv/3'>Mg coordination site</scene>.
+TetR binds DNA with a helix-turn-helix motif. The <scene name='47/477771/Cv/4'>inhibitor TC binds in the active site to several TetR side chains and to an octahedraly-coordinated Mg+2 ion</scene> <ref>PMID:8153629</ref>. Water molecules are shown as red spheres. <scene name='47/477771/Cv/5'>Mg coordination site</scene>.
 </StructureSection>
 == 3D Structures of tetracycline repressor protein==