Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution

Nature

Volumn 402, Issue 6760, 1999, Pages 377-385

  Lancaster, C Roy D ^a   Kröger, Achim ^b   Auer, Manfred ^a,c   Michel, Hartmut ^a  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^b GOETHE UNIVERSITY   (Germany)

^c NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B; FLAVINE ADENINE NUCLEOTIDE; FUMARATE REDUCTASE; FUMARIC ACID; IRON SULFUR PROTEIN;

ARTICLE; CRYSTAL STRUCTURE; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; NONHUMAN; PRIORITY JOURNAL; REDUCTION; WOLINELLA;

CELL MEMBRANE; CRYSTALLOGRAPHY, X-RAY; DICARBOXYLIC ACIDS; ELECTRON TRANSPORT; ESCHERICHIA COLI; FLAVIN-ADENINE DINUCLEOTIDE; HEME; IRON-SULFUR PROTEINS; METALS; MODELS, MOLECULAR; OXIDATION-REDUCTION; PROTEIN BINDING; PROTEIN CONFORMATION; QUINONES; SOLUBILITY; SUCCINATE DEHYDROGENASE; WOLINELLA;

BACTERIA (MICROORGANISMS); WOLINELLA; WOLINELLA SUCCINOGENES;

EID: 0010049951     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/46483     Document Type: Article

References (50)

1. Saraste, M. Oxidative phosphorylation at the fin de siècle. Science 283, 1488-1493 (1999).
2. Kröger, A. Fumarate as terminal acceptor of phosphorylative electron transport. Biochim. Biophys. Acta 595, 129-145 (1978).
3. Kröger, A. et al. Bacterial fumarate respiration. Arch. Microbiol. 158, 311-314 (1992).
4. Hägerhäll, C. Succinate:quinone oxidoreductases. Variations on a conserved theme. Biochim. Biophys. Acta 1320, 107-141 (1997).
5. Iverson, T. M., Luna-Chavez, C., Cecchini, G. & Rees, D. C. Structure of the Escherichia coli fumarate reductase respiratory complex. Science 284, 1961-1966 (1999).
6. Lauterbach, F. et al. The fumarate reductase operon of Wolinella succinogenes. Sequence and expression of the frdA and frdB genes. Arch. Microbiol. 154, 386-393 (1990).
7. Iwata, S., Ostermeier, C., Ludwig, B. & Michel, H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376, 660-669 (1995).
8. Kuriyan, J. et al. Convergent evolution of similar function in two structurally divergent enzymes. Nature 352, 172-174 (1991).
9. Holm, L. & Sander, C. Mapping the protein universe. Science 273, 595-602 (1996).
10. Mattevi, A. et al. Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/ fumarate reductase oxidoreductase family. Structure 7, 745-756 (1999).
11. Singer, T. P. & McIntire, W. S. Covalent attachment of flavin to flavoproteins: Occurrence, assay, and synthesis. Methods Enzymol. 106, 369-378 (1984).
12. Cole, S. T., Condon, C., Lemire, B. D. & Weiner, J. H. Molecular biology, biochemistry and bioenergetics of fumarate reductase, a complex membrane-bound iron-sulfur flavoenzyme of Escherichia coli. Biochim. Biophys. Acta 811, 381-403 (1985).
13. Kenny, W. C. & Kröger, A. The covalently bound flavin of Vibrio succinogenes succinate dehydrogenase. FEBS Lett. 73, 239-243 (1977).
14. van Hellemond, J. J. & Tielens, A. G. M. Expression and functional properties of fumarate reductase. Biochem. J. 304, 321-331 (1994).
15. Schröder, I. et al. Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis. J. Biol. Chem. 266, 13572-13579 (1991).
16. Unden, G. & Kröger, A. An essential sulfhydryl group at the substrate binding site of the fumarate reductase of Vibrio succinogenes. FEBS Lett. 117, 323-326 (1980).
17. Tomb, J.-F. et al. The complete genome sequence of the gastric pathogen Helicobacter pylori. Nature 388, 539-547 (1997).
18. Flachmann, R. et al. Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolate synthesis genes nadA and nadB. Eur. J. Biochem. 175, 221-228 (1988).
19. Vik, S. B. & Hatefi, Y. Possible occurrence and role of an essential histidyl residue in succinate dehydrogenase. Proc. Natl Acad. Sci. USA 78, 6749-6753 (1981).
20. Tsukihara, T. et al. Structure of the [2Fe-2S] ferredoxin 1 from Aphantothece sacrum at 2.2 Ångstroms resolution. J. Mol. Biol. 216, 399-410 (1990).
21. Körtner et al. Wolinella succinogenes fumarate reductase contains a dihaem cytochrome b. Mol. Microbiol. 4, 855-860 (1990).
22. Hägerhäll, C. & Hederstedt, L. A structural model for the membrane-integral domain of succinate:quinone oxidoreductases. FEBS Lett. 389, 25-31 (1996).
23. Simon, J. et al. Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon. Eur. J. Biochem. 251, 418-426 (1998).
24. Xia, D. et al. Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria. Science 277, 60-66 (1997).
25. Unden, G., Albracht, S. P. J. & Kröger, A. Redox potentials and kinetic properties of fumarate reductase complex from Vibrio succinogenes. Biochim. Biophys. Acta 767, 460-469 (1984).
26. Salerno, J. C. Electron transfer in succinate:ubiquinone reductase and quinol:fumarate reductase. Biochem. Soc. Trans. 19, 599-605 (1991).
27. Lancaster, C. R. D. Quinone-binding sites in membrane proteins: what can we learn from the Rhodopseudomonas viridis reaction centre? Biochem. Soc. Trans. 27, 591-596 (1999).
28. 2. Science 284, 1941-1942 (1999).
29. Bronder, M., Mell, H., Stupperich, E. & Kröger, A. Biosynthetic pathways of Vibrio succinogenes growing with fumarate as terminal electron acceptor and sole carbon source. Arch. Microbiol. 131, 213-223 (1982).
30. Unden, G., Hackenberg, H. & Kröger, A. Isolation and functional aspects of the fumarate reductase involved in the phosphorylative electron transport of Vibrio succinogenes. Biochim. Biophys. Acta 591, 275-288 (1980).
31. Tsiotis, G. in A Practical Guide to Membrane Protein Purification (eds von Jagow, G. & Schägger, H.) 149-159 (Academic, San Diego, 1994).
32. McPherson, A. Crystallization of Biological Macromolecules 304-305 (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, 1999).
33. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
34. Collaborative Computation Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
35. De La Fortelle, E. & Bricogne, G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494 (1997).
36. Otwinowski, Z. in Proc. CCP4 Study Weekend, 25-26 Jan 1991, Isomorphous Replacement and Anomalous Scattering (eds Wolf, W., Evans, P. R. & Leslie, A. G. W.) 80-86 (SERC Daresbury Laboratory, Warrington, UK, 1991).
37. Cowtan, K. dm: An automated procedure for phase improvement by density modification. Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography 30, 34-38 (1994).
38. 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 within these models. Acta Crystallogr. A 47, 110-119 (1991).
39. Brünger, A. T. et al. Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
40. Brünger, A. T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475 (1992).
41. Kleywegt, G. J. & Brünger, A. T. Checking your imagination: Applications of the free R value. Structure 4, 897-904 (1996).
42. Luzzati, P. V. Traitement statistique des erreurs dans la détermination des structures cristallines. Acta Crystallogr. 5, 802-810 (1952).
43. Read, R. J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140-149 (1986).
44. Engh, R. H. & Huber, R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A 47, 392-400 (1991).
45. B. Structure 5, 1339-1359 (1997).
46. Kraulis, P. J. MolScript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
47. Esnouf, R. M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graphics Mod. 15, 132-134 (1997).
48. Esnouf, R. M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D 55, 938-940 (1999).
49. Kabsch, W. & Sander, C. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637 (1983).
50. Merritt, E. A. & Bacon, D. J. Raster3D: Photorealistic molecular graphics. Methods Enzymol. 277, 505-524 (1997).