MAD structure of Pseudomonas nautica dimeric cytochrome C552 mimicks the C4 dihemic cytochrome domain association

Journal of Molecular Biology

Volumn 289, Issue 4, 1999, Pages 1017-1028

  Brown, Kieron ^a   Nurizzo, Didier ^a   Besson, Stephane ^c   Shepard, William ^b   Moura, Jose ^c   Moura, Isabel ^c   Tegoni, Mariella ^a   Cambillau, Christian ^a  

^a Centre National de la Recherche Scientifique   (France)

^b UNIVERSITÉ PARIS SACLAY   (France)

^c UNIVERSIDADE NOVA DE LISBOA   (Portugal)

Author keywords

Cytochrome c; Heme; Multiple wavelength anomalous dispersion (MAD); Pseudomonas; X ray structure

Indexed keywords

CYTOCHROME C; DIMER;

ARTICLE; CHROMATIUM VINOSUM; CRYSTALLOGRAPHY; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; PSEUDOMONAS; PSEUDOMONAS STUTZERI;

ALLOCHROMATIUM VINOSUM; CHROMATIUM; CHROMATIUM VINOSUM; MARINOBACTER HYDROCARBONOCLASTICUS; NEGIBACTERIA; PSEUDOMONAS; PSEUDOMONAS AERUGINOSA; PSEUDOMONAS NAUTICA; PSEUDOMONAS STUTZERI;

EID: 0032981135     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2838     Document Type: Article

References (27)

1. Bonin P., Gilewicz M., Bertrand J. C. Denitrification by a marine bacterium Pseudomonas nautica strain 617. Ann. Inst. Pasteur Microbiol. 138:1987;371-383.
2. Brünger A. T., Kuriyan J., Karplus M. X-PLOR: crystallographic R -factor refinement by molecular dynamics. Science. 235:1987;458-460.
3. Chen Z.-w., Monjoo Koh, Van Driessche G., Van Beeumen J. J., Bartsch R., Meyer T. E., Cusanovich M. A., Mathew F. S. The structure determination of flavocytochrome c sulphide dehydrogenase from a purple phototrophic bacterium. Science. 266:1994;430-432.
4. Acta Crystallog. sect. D. 50:1994;760-766.
5. Fauque G., Moura J. J. G., Besson S., Saraiva L. M., Moura I. Caractérisation préliminaire du système cytochromique de la bactérie marine dénitrifiante Pseudomonas nautica. Océanis. 18:1992;211-216.
6. Ferguson S. J. Denitrification: a question of the control and organisation of electron and ion transport. Trends Biochem. Sci. 12:1987;354-357.
7. Janin J. Specific versus non-specific contacts in protein crystals. Nature Struct. Biol. 4:1997;973-974.
8. 4from Pseudomonas stutzeri determined at 2.2 Å resolution. Structure. 5:1997;203-216.
9. Krishna Murphy H. M., Hendrickson W. A., Orme-Johnson W. H., Merritt E. A., Phizackerly R. P. Crystal structure of Clostridium acidi-urici ferredoxin at 5 Å resolution based on measurements of anomalous X-ray scattering at multiple wavelengths. J. Biol. Chem. 263:1988;18430-18436.
10. Laskowski R., MacArthur M., Moss D., Thornton J. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;91-97.
11. 551from Pseudomonas aeruginosa at 1.6 Å resolution and comparison of the two redox forms. J. Mol. Biol. 156:1982;389-409.
12. Matthews B. W. Solvent content of crystals. J. Mol. Biol. 33:1968;491-497.
13. Navaza J. AMoRe: an automated package for molecular replacement. Acta. Crystallog. sect. A. 50:1994;157-163.
14. Nurizzo D., Silvestrini M-C., Mathieu M., Cutruzzolà F., Bourgeois D., Fulop V., Hajdu J., Brunori M., Tegoni M., Cambillau C. N-terminal arm exchange is observed in the 2.15 Å crystal structure of oxidised nitrite reductase fromPseudomonas aeruginosa. Structure. 5:1997;1157-1171.
15. Otwinowski Z. DENZO: oscillation data reduction program. Sawyer L., Isaacs N. W., Bailey S. Data Collection and Processing. 1993;56-63 DLSCI/R34Daresbury Laboratory.
16. Pelletier H., Kraut J. Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochromec. Science. 258:1992;1748-1755.
17. Ravelli R. B. G., Sweet R. M., Skinner J. M., Duisenberg A. J. M., Kroon J. STRATEGY: a program to optimize the starting spindle angle and scan range for X-ray data collection. J. Appl. Crystallog. 30:1997;551.
18. Roussel A., Cambillau C. The Turbo frodo graphics package. Silicon Graphics. Silicon Graphics Geometry Partners Directory. 1991.
19. Saraiva L. M., Besson S., Fauque G., Moura I. Characterization of the dihemic cytochrome c 549 from the marine denitrifying bacterium Pseudomonas nautica 617. Biochem. Biophys. Res. Commun. 199:1994a;1289-1296.
20. 552fromPseudomonas nautica 617. Eur. J. Biochem. 224:1994b;1011-1017.
21. Sheldrick G. M. Phase annealing in SHELX-90: direct methods for larger structures. Acta Crystallog. sect. A. 46:1990;467.
22. Smith J. L., Zaluzec E. J., Wery J.-P., Niu L., Switzer R. L., Zalkin H., Satow Y. Structure of the allostric regulatory enzyme of purine biosynthesis. Science. 264:1994;1427-1433.
23. 552: a new highly thermostable cytochrome-c structure obtained by MAD phasing. J. Mol. Biol. 271:1997;629-644.
24. Thompson J. D., Higgins D. G., Gibson T. J. CLUSTALW: improving the sensitivity of progressive multiple sequence alignment weighting, position specific gap penalties and weight matrix choice. Nucl. Acids Res. 22:1994;4673-4680.
25. Vijgenboom E., Busch J. E., Canters G. W. In vivo studies disprove an obligatory role of azurin in denitrification in Pseudomonas aeruginosa and show that azu expression is under control of rpos and anr. Microbiology. 143:1997;2853-2863.
26. Wang B. C. Resolution of phase ambiguity in macromolecular crystallography. Wyckoff H. W., Hirs C. H. W., Timasheff S. N. Methods in Enzymology. 1985;90-112 Academic Press.
27. Zhang K. Y. J., Main P. The use of Sayre's equation with solvent flattening and histogram matching for phase extension and refinement of protein structures. Acta Crystallog. sect. A. 46:1990;377.