1a6i
From Proteopedia
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'''TET REPRESSOR, CLASS D VARIANT''' | '''TET REPRESSOR, CLASS D VARIANT''' | ||
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[[Category: Saenger, W.]] | [[Category: Saenger, W.]] | ||
[[Category: Schnappinger, D.]] | [[Category: Schnappinger, D.]] | ||
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- | [[Category: | + | [[Category: Repressor]] |
- | [[Category: | + | [[Category: Transcription regulation]] |
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Revision as of 06:53, 2 May 2008
TET REPRESSOR, CLASS D VARIANT
Overview
The X-ray crystal structure analysis of inducer-free Tet repressor, TetR, at 2.4 A resolution identifies one of two openings of the tunnel-like binding site as the entrance for the inducer tetracycline-Mg2+, [Mg Tc]+. Recognition and binding of the inducer unleashes conformational changes leading to the induced state of TetR. In the first step, the C-terminal turn of alpha-helix 6 unwinds, thereby altering the orientation of alpha-helix 4. This different orientation of alpha-helix 4 is stabilized by a series of hydrogen bonds mediated through a chain of eight water molecules. The alpha-helix 4 connects the DNA-binding domain (alpha-helices 1 to 3) to the rigid TetR core, and thus regulates gene expression through its respective orientations.
About this Structure
1A6I is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Conformational changes of the Tet repressor induced by tetracycline trapping., Orth P, Cordes F, Schnappinger D, Hillen W, Saenger W, Hinrichs W, J Mol Biol. 1998 Jun 5;279(2):439-47. PMID:9642048 Page seeded by OCA on Fri May 2 09:53:22 2008