A direct photo-activated affinity modification of tetracycline transcription repressor protein TetR(D) with tetracycline

被引：3

作者：

Beliakova, MM

Anokhina, MM

Spiridonova, VA

Dobrov, EN

Egorov, TA

Wittmann-Liebold, B

Orth, P

Saenger, W

Kopylov, AM ^{[1
]}

机构：

[1] Moscow MV Lomonosov State Univ, Dept Chem, Moscow 119899, Russia

[2] Moscow MV Lomonosov State Univ, AN Belozersky Inst Phys Chem Biol, Moscow 119899, Russia

[3] Russian Acad Sci, MM Shemyakin Bioorgan Chem Inst, Moscow, Russia

[4] Russian Acad Sci, YA Ovchinnikov Inst Bioorgan Chem, Moscow, Russia

[5] Max Delbruck Ctr Mol Med, Berlin, Germany

[6] Free Univ Berlin, Inst Crystallog, D-1000 Berlin, Germany

来源：

FEBS LETTERS | 2000年 / 477卷 / 03期

基金：

俄罗斯基础研究基金会;

关键词：

tetracycline; transcription repressor protein TetR(D); photo-activated affinity modification; protein sequencing; binding site;

D O I：

10.1016/S0014-5793(00)01728-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：263 / 267

页数：5

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