A direct photo-activated affinity modification of tetracycline transcription repressor protein TetR(D) with tetracycline(1).
Results of a first successful application of a direct photo-induced affinity modification of Tet repressor (TetR(D)) protein with tetracycline within a complex of known three-dimensional structure are described. The conditions of the modification have provided suitable yields of the modified complex and allowed characterization of the modified segments of the protein. The potential of tetracycline as a fine modifying reagent was established. In the complex of TetR(D) protein with tetracycline, the antibiotic modifies at least two segments, Ile59-Glu73 and Ala173-Glu183, which form a binding tunnel for the drug according to the X-ray analysis. These data open possibilities for the use of different tetracycline targets for structural studies in solution.
Beliakova
M M
MM
Department of Chemistry, Moscow State University, 119899 Moscow, Russia.
Anokhina
M M
MM
Spiridonov
V A
VA
Dobrov
E N
EN
Egorov
T A
TA
Wittmann-Liebold
B
B
Orth
P
P
Saenger
W
W
Kopylov
A M
AM
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D019920:Photoaffinity Labels; D012097:Repressor Proteins / Q000737:chemistry*; D013752:Tetracycline / Q000737:chemistry*; D014961:X-Ray Diffraction
D019920:Photoaffinity Labels; D012097:Repressor Proteins; C034811:tetracycline resistance-encoding transposon repressor protein; D013752:Tetracycline