Crystal structure of the tet repressor in complex with a novel tetracycline, 9-(N,N-dimethylglycylamido)- 6-demethyl-6-deoxy-tetracycline.

TitleCrystal structure of the tet repressor in complex with a novel tetracycline, 9-(N,N-dimethylglycylamido)- 6-demethyl-6-deoxy-tetracycline.
Publication TypeJournal Article
Year of Publication1999
AuthorsOrth P, Schnappinger D, Sum PE, Ellestad GA, Hillen W, Saenger W, Hinrichs W
JournalJ Mol Biol
Volume285
Issue2
Pagination455-61
Date Published1999 Jan 15
ISSN0022-2836
KeywordsCrystallography, X-Ray, Macromolecular Substances, Molecular Structure, Mutagenesis, Protein Conformation, Repressor Proteins, Tetracyclines
Abstract

The tetracycline analog 9-(N, N-dimethylglycylamido)-6-demethyl-6-deoxy-tetracycline (9glyTc) belongs to a new group of tetracyclines called glycylcyclines. They are strong antibiotics showing reduced sensitivity against the major tetracycline resistance mechanisms. We have determined the crystal structure of 9glyTc in complex with Tet repressor class D, TetR(D), at 2.4 A resolution. Sterical hindrance at the entrance of the tetracycline binding tunnel of TetR by the bulky and charged glycyl amido substituent interferes with conformational changes required for the mechanism of induction, and leads to decreased induction efficiency as observed for point mutations of amino acid residues located in the neighbourhood to the glycylamido moiety of bound 9glyTc.

DOI10.1006/jmbi.1998.2290
Alternate JournalJ Mol Biol
PubMed ID9878420

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