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1du7

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{{STRUCTURE_1du7| PDB=1du7 | SCENE= }}
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'''CRYSTAL STRUCTURE OF TET REPRESSOR CLASS D WITH 4-EPI-TETRACYCLINE'''
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===CRYSTAL STRUCTURE OF TET REPRESSOR CLASS D WITH 4-EPI-TETRACYCLINE===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_10700280}}
==About this Structure==
==About this Structure==
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[[Category: Hth-motif]]
[[Category: Hth-motif]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:16:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:37:22 2008''

Revision as of 20:37, 30 June 2008

Image:1du7.png

Template:STRUCTURE 1du7

CRYSTAL STRUCTURE OF TET REPRESSOR CLASS D WITH 4-EPI-TETRACYCLINE

Template:ABSTRACT PUBMED 10700280

About this Structure

1DU7 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

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