1a6i: Difference between revisions
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[[Image:1a6i.gif|left|200px]] | [[Image:1a6i.gif|left|200px]] | ||
'''TET REPRESSOR, CLASS D VARIANT''' | {{Structure | ||
|PDB= 1a6i |SIZE=350|CAPTION= <scene name='initialview01'>1a6i</scene>, resolution 2.4Å | |||
|SITE= <scene name='pdbsite=TNE:Empty+Tetracycline+Binding+Tunnel'>TNE</scene> | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''TET REPRESSOR, CLASS D VARIANT''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1A6I is a [ | 1A6I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6I OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9642048 9642048] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:53:42 2008'' |
Revision as of 10:53, 20 March 2008
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, resolution 2.4Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
TET REPRESSOR, CLASS D VARIANT
OverviewOverview
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 StructureAbout this Structure
1A6I is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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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