2vpr
From Proteopedia
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|PDB= 2vpr |SIZE=350|CAPTION= <scene name='initialview01'>2vpr</scene>, resolution 2.49Å | |PDB= 2vpr |SIZE=350|CAPTION= <scene name='initialview01'>2vpr</scene>, resolution 2.49Å | ||
|SITE= <scene name='pdbsite=AC1:Binding+Site+For+Residue+Tdc+A+1206'>AC1</scene>, <scene name='pdbsite=AC2:Binding+Site+For+Residue+Mg+A+1207'>AC2</scene> and <scene name='pdbsite=AC3:Binding+Site+For+Residue+So4+A+1208'>AC3</scene> | |SITE= <scene name='pdbsite=AC1:Binding+Site+For+Residue+Tdc+A+1206'>AC1</scene>, <scene name='pdbsite=AC2:Binding+Site+For+Residue+Mg+A+1207'>AC2</scene> and <scene name='pdbsite=AC3:Binding+Site+For+Residue+So4+A+1208'>AC3</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TDC:5A,6-ANHYDROTETRACYCLINE'>TDC</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vpr OCA], [http://www.ebi.ac.uk/pdbsum/2vpr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vpr RCSB]</span> | ||
}} | }} | ||
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[[Category: Palm, G.]] | [[Category: Palm, G.]] | ||
[[Category: Schuldt, L.]] | [[Category: Schuldt, L.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: TDC]] | ||
[[Category: antibiotic resistance]] | [[Category: antibiotic resistance]] | ||
[[Category: dna-binding]] | [[Category: dna-binding]] | ||
| Line 38: | Line 38: | ||
[[Category: transcription regulator]] | [[Category: transcription regulator]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:14:02 2008'' |
Revision as of 02:14, 31 March 2008
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| , resolution 2.49Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TET REPRESSOR CLASS H IN COMPLEX WITH 5A,6-ANHYDROTETRACYCLINE-MG
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
2VPR is a Single protein structure of sequence from Pasteurella multocida. 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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