1a6i

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{{STRUCTURE_1a6i| PDB=1a6i | SCENE= }}
{{STRUCTURE_1a6i| PDB=1a6i | SCENE= }}
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'''TET REPRESSOR, CLASS D VARIANT'''
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===TET REPRESSOR, CLASS D VARIANT===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9642048 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9642048}}
==About this Structure==
==About this Structure==
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[[Category: Repressor]]
[[Category: Repressor]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:14:54 2008''

Revision as of 13:14, 30 June 2008

Image:1a6i.png

Template:STRUCTURE 1a6i

TET REPRESSOR, CLASS D VARIANT

Template:ABSTRACT PUBMED 9642048

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

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