1qpi

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[[Image:1qpi.gif|left|200px]]
[[Image:1qpi.gif|left|200px]]
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{{Structure
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|PDB= 1qpi |SIZE=350|CAPTION= <scene name='initialview01'>1qpi</scene>, resolution 2.50&Aring;
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The line below this paragraph, containing "STRUCTURE_1qpi", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>
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{{STRUCTURE_1qpi| PDB=1qpi | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qpi OCA], [http://www.ebi.ac.uk/pdbsum/1qpi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qpi RCSB]</span>
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'''CRYSTAL STRUCTURE OF TETRACYCLINE REPRESSOR/OPERATOR COMPLEX'''
'''CRYSTAL STRUCTURE OF TETRACYCLINE REPRESSOR/OPERATOR COMPLEX'''
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[[Category: Saenger, W.]]
[[Category: Saenger, W.]]
[[Category: Schnappinger, D.]]
[[Category: Schnappinger, D.]]
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[[Category: repressor/operator complex]]
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[[Category: Repressor/operator complex]]
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[[Category: transcription regulation]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:33:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:17:10 2008''
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Revision as of 03:33, 3 May 2008

Image:1qpi.gif

Template:STRUCTURE 1qpi

CRYSTAL STRUCTURE OF TETRACYCLINE REPRESSOR/OPERATOR COMPLEX


Overview

The tetracycline repressor (TetR) regulates the most abundant resistance mechanism against the antibiotic tetracycline in grain-negative bacteria. The TetR protein and its mutants are commonly used as control elements to regulate gene expression in higher eukaryotes. We present the crystal structure of the TetR homodimer in complex with its palindromic DNA operator at 2.5 A resolution. Comparison to the structure of TetR in complex with the inducer tetracycline-Mg2+ allows the mechanism of induction to be deduced. Inducer binding in the repressor core initiates conformational changes starting with C-terminal unwinding and shifting of the short helix a6 in each monomer. This forces a pendulum-like motion of helix a4, which increases the separation of the attached DNA binding domains by 3 A, abolishing the affinity of TetR for its operator DNA.

About this Structure

1QPI is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural basis of gene regulation by the tetracycline inducible Tet repressor-operator system., Orth P, Schnappinger D, Hillen W, Saenger W, Hinrichs W, Nat Struct Biol. 2000 Mar;7(3):215-9. PMID:10700280 Page seeded by OCA on Sat May 3 06:33:20 2008

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