1qpi
From Proteopedia
(New page: 200px<br /><applet load="1qpi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qpi, resolution 2.50Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1qpi.gif|left|200px]]<br /><applet load="1qpi" size=" | + | [[Image:1qpi.gif|left|200px]]<br /><applet load="1qpi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qpi, resolution 2.50Å" /> | caption="1qpi, resolution 2.50Å" /> | ||
'''CRYSTAL STRUCTURE OF TETRACYCLINE REPRESSOR/OPERATOR COMPLEX'''<br /> | '''CRYSTAL STRUCTURE OF TETRACYCLINE REPRESSOR/OPERATOR COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The tetracycline repressor (TetR) regulates the most abundant resistance | + | 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== | ==About this Structure== | ||
| - | 1QPI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with IMD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1QPI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QPI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:16 2008'' |
Revision as of 12:42, 21 February 2008
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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 with as ligand. 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 Thu Feb 21 14:42:16 2008
