2trt

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(New page: 200px<br /><applet load="2trt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2trt, resolution 2.5&Aring;" /> '''TETRACYCLINE REPRESSO...)
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'''TETRACYCLINE REPRESSOR CLASS D'''<br />
'''TETRACYCLINE REPRESSOR CLASS D'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2TRT 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 MG and TAC as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1TRT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2TRT OCA].
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2TRT 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=MG:'>MG</scene> and <scene name='pdbligand=TAC:'>TAC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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==
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[[Category: transcription regulation]]
[[Category: transcription regulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 14:06:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:50:03 2008''

Revision as of 16:50, 21 February 2008


2trt, resolution 2.5Å

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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 with and as ligands. 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

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