Crystallographic structure and biochemical analysis of the Thermus thermophilus osmotically inducible protein C

Journal of Molecular Biology

Volumn 338, Issue 5, 2004, Pages 959-968

  Rehse, Peter H ^a   Ohshima, Noriyasu ^a   Nodake, Yuichi ^a   Tahirov, Tahir H ^a  

^a RIKEN HARIMA INSTITUTE   (Japan)

Author keywords

CHP, cumene hydroperoxide; DTT, 1,4 dithiothreitol; Ohr; Ohr, organic hydroperoxide resistance protein; OsmC; OsmC, osmotically inducible protein C; Osmotic stress; Peroxidase; tBOOH, tert butyl hydroperoxide; X ray crystal structure

Indexed keywords

ARGININE; BACTERIAL PROTEIN; CYSTEINE; DIMER; GLUTAMIC ACID; MONOMER; OSMOTICALLY INDUCIBLE PROTEIN C; PEROXIDASE; PROTEIN C; SELENOMETHIONINE; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BETA SHEET; CONTROLLED STUDY; ENZYME ACTIVITY; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN INDUCTION; PROTEIN STRUCTURE; THERMOPHILIC BACTERIUM; THERMUS THERMOPHILUS; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); CHANDIPURA VIRUS; THERMUS; THERMUS THERMOPHILUS;

EID: 2142652096     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.03.050     Document Type: Article

References (28)

1. Hengge-Aronis R. Back to log phase: sigma S as a global regulator in the osmotic control of gene expression in Escherichia coli. Mol. Microbiol. 21:1996;887-893.
2. Kolter R., Siegele D.A., Tormo A. The stationary phase of the bacterial life cycle. Annu. Rev. Microbiol. 47:1993;855-874.
3. McCann M.P., Kidwell J.P., Matin A. The putative sigma factor KatF has a central role in development of starvation-mediated general resistance in Escherichia coli. J. Bacteriol. 173:1991;4188-4194.
4. Gutierrez C., Devedjian J.C. Osmotic Induction of gene osmC expression in Escherichia coli K12. J. Mol. Biol. 20:1991;959-973.
5. B- dependent general stress regulon. J. Bacteriol. 180:1998;4212-4218.
6. Bouvier J., Gordia S., Kampmann G., Lange R., Hengge-Aronis R., Gutierrez C. Interplay between global regulators of Escherichia coli: effect of RpoS, Lrp and H-NS on transcription of the gene osmC. Mol. Microbiol. 28:1998;971-980.
7. Cp1, a promoter of the stress-inducible gene osmC in Escherichia coli. Microbiology. 147:2001;2795-2803.
8. Davalos-Garcia M., Conter A., Toesca I., Gutierrez C., Cam K. Regulation of osmC gene expression by the two-component system rcsB-rcsC in Escherichia coli. J. Bacteriol. 183:2001;5870-5876.
9. Atichartpongkul S., Loprasert S., Vattanaviboon P., Whangsuk W., Helmann J.D., Mongkolsuk S. Bacterial Ohr and OsmC paralogues define two protein families with distinct functions and patterns of expression. Microbiology. 147:2001;1775-1782.
10. Conter A., Gangneux C., Suzanne M., Gutierrez C. Survival of Escherichia coli during long-term starvation: effects of aeration, NaCl, and the rpoS and osmC gene products. Res. Microbiol. 152:2001;17-26.
11. Mongkolsuk S., Praituan W., Loprasert S., Fuangthong M., Chamnongpol S. Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv Phaseoli. J. Bacteriol. 180:1998;2636-2643.
12. Lesniak J., Barton W.A., Nikolov D.B. Structural and functional characterization of the Pseudomonas hydroperoxide resistance protein Ohr. EMBO J. 21:2002;6649-6659.
13. Rehse P.H., Nodake Tahirov T.H. Expression, purification crystallization and preliminary crystallographic analysis of Osmotically Inducible Protein C. Acta Crystallog. sect. D. 60:2003;357-358.
14. Pflugrath J.W. The finer things in X-ray diffraction data collection. Acta Crystallog sect. D. 55:1999;1718-1725.
15. Brünger A.T., Adams P.D., Clore G.M., Delano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography and NMR system (CNS): a new software system for macromolecular structure determination. Acta Crystallog. sect. D. 54:1998;905-921.
16. Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
17. Terwilliger T.C., Berendzen J. Automated MAD and MIR structure solution. Acta Crystallog. sect. D. 55:1999;849-861.
18. Terwilliger T.C. Maximum-likelihood density modification with pattern recognition of structural motifs. Acta Crystallog. sect. D. 57:2001;1755-1762.
19. Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D. 53:1997;240-245.
20. Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
21. Kraulis J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
22. Esnouf R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. J. Acta Crystallog. sect. D. 55:1999;938-940.
23. Merritt E.A., Bacon D.J. Raster3D: Photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
24. Nicholls A., Sharp K., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
25. Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22:1994;4673-4680.
26. Wolff S. Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxidases. Methods Enzymol. 233:1994;182-189.
27. Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
28. Gouet P., Courcelle E., Stuart D.I., Metoz F. ESPript: multiple sequence alignments in PostScript. Bioinformatics. 15:1999;305-308.