2trt

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{{STRUCTURE_2trt| PDB=2trt | SCENE= }}
{{STRUCTURE_2trt| PDB=2trt | SCENE= }}
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'''TETRACYCLINE REPRESSOR CLASS D'''
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===TETRACYCLINE REPRESSOR CLASS D===
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==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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{{ABSTRACT_PUBMED_8153629}}
==About this Structure==
==About this Structure==
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[[Category: Repressor]]
[[Category: Repressor]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:35:36 2008''

Revision as of 12:35, 28 July 2008

Image:2trt.png

Template:STRUCTURE 2trt

TETRACYCLINE REPRESSOR CLASS D

Template:ABSTRACT PUBMED 8153629

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 Mon Jul 28 15:35:36 2008

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