Crystal structure of the TetR/CamR family repressor Mycobacterium tuberculosis EthR implicated in ethionamide resistance

Journal of Molecular Biology

Volumn 340, Issue 5, 2004, Pages 1095-1105

  Dover, Lynn G ^a   Corsino, Patrick E ^a   Daniels, Ian R ^a   Cocklin, Sarah L ^b   Tatituri, Vijaya ^a   Besra, Gurdyal S ^a   Fütterer, Klaus ^a  

^a UNIVERSITY OF BIRMINGHAM   (United Kingdom)

^b UNIVERSITY OF SUNDERLAND   (United Kingdom)

Author keywords

BVMO, Baeyer Villiger monooxygenase; ETH, ethionamide; ethionamide; helix turn helix; HTH, helix turn helix; INH, isoniazid; MDR TB, multiple drug resistant Mycobacterium tuberculosis; Mycobacterium tuberculosis; TetR family; X ray crystallography

Indexed keywords

BUFFER; DIOXANE; ETHIONAMIDE; ETHIONAMIDE A; ETHIONAMIDE R; LIGAND; REPRESSOR PROTEIN; SPACER DNA; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

ANTIBIOTIC RESISTANCE; ARCHITECTURE; ARTICLE; BACTERIAL GENOME; BAEYER VILLIGER REACTION; BINDING AFFINITY; BINDING SITE; COMPARATIVE STUDY; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; DNA BINDING; DRUG BINDING SITE; ESCHERICHIA COLI; GENE ACTIVATION; GENE REPRESSION; GENETIC TRANSCRIPTION; HYDROPHOBICITY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN STRUCTURE; REPRESSOR GENE; STAPHYLOCOCCUS AUREUS;

ESCHERICHIA COLI; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS; STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS;

EID: 3242812945     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.06.003     Document Type: Article

References (36)

1. Kremer L., Besra G.S. Current status and future development of antitubercular chemotherapy. Expert Opin. Investig. Drugs. 11:2002;1033-1049
2. Mahmoudi A., Iseman M.D. Pitfalls in the care of patients with tuberculosis. Common errors and their association with the acquisition of drug resistance. J. A. Med. Assoc. 270:1993;65-68
3. Jenner P.J., Smith S.E. Plasma levels of ethionamide and prothionamide in a volunteer following intravenous and oral dosages. Lepr. Rev. 58:1987;31-37
4. Larsen M.H., Vilcheze C., Kremer L., Besra G.S., Parsons L., Salfinger M., et al. Overexpression of inhA, but not kasA, confers resistance to isoniazid and ethionamide in Mycobacterium smegmatis, M. bovis BCG and M. tuberculosis. Mol. Microbiol. 46:2002;453-466
5. Fattorini L., Iona E., Ricci M.L., Thoresen O.F., Orru G., Oggioni M.R., et al. Activity of 16 antimicrobial agents against drug-resistant strains of Mycobacterium tuberculosis. Microb. Drug Resist. 5:1999;265-270
6. Banerjee A., Dubnau E., Quemard A., Balasubramanian V., Um K.S., Wilson T., et al. inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis. Science. 263:1994;227-230
7. Zhang Y., Heym B., Allen B., Young D., Cole S. The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature. 358:1992;591-593
8. Baulard A.R., Betts J.C., Engohang-Ndong J., Quan S., McAdam R.A., Brennan P.J., et al. Activation of the pro-drug ethionamide is regulated in mycobacteria. J. Biol. Chem. 275:2000;28326-28331
9. DeBarber A.E., Mdluli K., Bosman M., Bekker L.G., Barry C.E. III. Ethionamide activation and sensitivity in multidrug-resistant Mycobacterium tuberculosis. Proc. Natl Acad. Sci. USA. 97:2000;9677-9682
10. Vannelli T.A., Dykman A., Ortiz De Montellano P.R. The antituberculosis drug ethionamide is activated by a flavoprotein monooxygenase. J. Biol. Chem. 277:2002;12824-12829
11. Fraaije M.W., Kamerbeek N.M., Heidekamp A.J., Fortin R., Janssen D.B. The prodrug activator EtaA from Mycobacterium tuberculosis is a Baeyer-Villiger monooxygenase. J. Biol. Chem. 279:2004;3354-3360
12. Engohang-Ndong J., Baillat D., Aumercier M., Bellefontaine F., Besra G.S., Locht C., et al. EthR, a repressor of the TetR/CamR family implicated in ethionamide resistance in mycobacteria, octamerizes cooperatively on its operator. Mol. Microbiol. 51:2004;175-188
13. Orth P., Schnappinger D., Hillen W., Saenger W., Hinrichs W. Structural basis of gene regulation by the tetracycline inducible Tet repressor-operator system. Nature Struct. Biol. 7:2000;215-219
14. + reveals mechanism of antibiotic resistance. J. Mol. Biol. 247:1995;260-280
15. Schumacher M.A., Miller M.C., Grkovic S., Brown M.H., Skurray R.A., Brennan R.G. Structural mechanisms of QacR induction and multidrug recognition. Science. 294:2001;2158-2163
16. Schumacher M.A., Miller M.C., Grkovic S., Brown M.H., Skurray R.A., Brennan R.G. Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR. EMBO J. 21:2002;1210-1218
17. Natsume R., Ohnishi Y., Senda T., Horinouchi S. Crystal structure of a gamma-butyrolactone autoregulator receptor protein in Streptomyces coelicolor A3(2). J. Mol. Biol. 336:2004;409-419
18. Collaborative computational project number 4. The CCP4 suite of programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763
19. Laneelle M.A., Laneelle G. Structure of mycolic acids and an intermediate in the biosynthesis of dicarboxylic mycolic acids. Eur. J. Biochem. 12:1970;296-300
20. Toriyama S., Imaizumi S., Tomiyasu I., Masui M., Yano I. Incorporation of O-18 into long-chain, secondary alcohols derived from ester mycolic acids in Mycobacterium Phlei. Biochim. Biophys. Acta. 712:1982;427-429
21. Asselineau C., Asselineau J., Laneelle G., Laneelle M.A. The biosynthesis of mycolic acids by mycobacteria: current and alternative hypotheses. Prog. Lipid Res. 41:2002;501-523
22. White S.A., Peake S.J., McSweeney S., Leonard G., Cotton N.P., Jackson J.B. The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria. Struct. Fold. Des. 8:2000;1-12
23. Evans G., Pettifer R.F. CHOOCH: a program for deriving anomalous-scattering factors from X-ray fluorescence spectra. J. Appl. Crystallog. 34:2001;82-86
24. Terwilliger T.C. Automated structure solution, density modification and model building. Acta Crystallog. sect. D. 58:2002;1937-1940
25. Perrakis A., Morris R., Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nature Struct. Biol. 6:1999;458-463
26. Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography & NMR system: a new software suite for macromolcular structure determination. Acta Crystallog. sect. D. 54:1998;905-921
27. Murshudov A., Vagin A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D. 53:1997;240-255
28. Winn M.D., Isupov M.N., Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallog. sect. D. 57:2001;122-133
29. Jones T.A., Thirup S. Using known substructures in protein model building and crystallography. EMBO J. 5:1986;819-822
30. Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119
31. Carson M. RIBBONS. Methods Enzymol. 277:1997;493-505
32. Laskowski R.A. SURFNET: a program for visualizing molecular surfaces, cavities, and intermolecular interactions. J. Mol. Graph. 13:1995;323-330. see also pp. 307-328
33. Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis. 18:1997;2714-2723
34. Lu G. A WWW service system for automatic comparison of protein structures. Protein Data Bank Quart. Newsletter. 78:1996;10-11
35. Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296
36. Engh R.A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A. 47:1991;392-400