2trt
From Proteopedia
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| - | [[Image:2trt.gif|left|200px]] | + | [[Image:2trt.gif|left|200px]] |
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| - | '''TETRACYCLINE REPRESSOR CLASS D''' | + | {{Structure |
| + | |PDB= 2trt |SIZE=350|CAPTION= <scene name='initialview01'>2trt</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=TAC:TETRACYCLINE'>TAC</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''TETRACYCLINE REPRESSOR CLASS D''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2TRT is a [ | + | 2TRT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry 1TRT. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TRT OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance., Hinrichs W, Kisker C, Duvel M, Muller A, Tovar K, Hillen W, Saenger W, Science. 1994 Apr 15;264(5157):418-20. PMID:[http:// | + | Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance., Hinrichs W, Kisker C, Duvel M, Muller A, Tovar K, Hillen W, Saenger W, Science. 1994 Apr 15;264(5157):418-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8153629 8153629] |
[[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 18:39:27 2008'' |
Revision as of 16:39, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TETRACYCLINE REPRESSOR CLASS D
Overview
The most frequently occurring resistance of Gram-negative bacteria against tetracyclines is triggered by drug recognition of the Tet repressor. This causes dissociation of the repressor-operator DNA complex and enables expression of the resistance protein TetA, which is responsible for active efflux of tetracycline. The 2.5 angstrom resolution crystal structure of the homodimeric Tet repressor complexed with tetracycline-magnesium reveals detailed drug recognition. The orientation of the operator-binding helix-turn-helix motifs of the repressor is inverted in comparison with other DNA binding proteins. The repressor-drug complex is unable to interact with DNA because the separation of the DNA binding motifs is 5 angstroms wider than usually observed.
About this Structure
2TRT is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1TRT. Full crystallographic information is available from OCA.
Reference
Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance., Hinrichs W, Kisker C, Duvel M, Muller A, Tovar K, Hillen W, Saenger W, Science. 1994 Apr 15;264(5157):418-20. PMID:8153629
Page seeded by OCA on Thu Mar 20 18:39:27 2008
