Structure of l-aspartate oxidase from the hyperthermophilic archaeon Sulfolobus tokodaii

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1784, Issue 3, 2008, Pages 563-571

  Sakuraba, Haruhiko ^a   Yoneda, Kazunari ^b   Asai, Issaku ^a   Tsuge, Hideaki ^c   Katunuma, Nobuhiko ^c   Ohshima, Toshihisa ^d  

^a UNIVERSITY OF TOKUSHIMA   (Japan)

^b TOKAI UNIVERSITY   (Japan)

^c TOKUSHIMA BUNRI UNIVERSITY   (Japan)

^d KYUSHU UNIVERSITY   (Japan)

Author keywords

Archaea; Crystal structure; Hyperthermophile; l Aspartate oxidase; Sulfolobus tokodaii; Thermostability

Indexed keywords

ASPARTATE OXIDASE; FLAVINE ADENINE NUCLEOTIDE;

ALPHA HELIX; ARTICLE; BETA CHAIN; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME STRUCTURE; HYPERTHERMOPHILIC ARCHAEON; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS; SULFOLOBUS; SULFOLOBUS TOKODAII; THERMOSTABILITY;

AMINO ACID OXIDOREDUCTASES; AMINO ACID SEQUENCE; ARCHAEAL PROTEINS; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; FLAVIN-ADENINE DINUCLEOTIDE; HEAT; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SULFOLOBUS;

ARCHAEA; ESCHERICHIA COLI; SULFOLOBUS TOKODAII;

EID: 43049099608     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.12.012     Document Type: Article

References (33)

1. Nasu S., Wicks F.D., and Gholson R.K. l-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase. J. Biol. Chem. 257 (1982) 626-632
2. + synthesis. Adv. Enzymol. Relat. Areas Mol. Biol. 73 (1999) 135-182
3. Foster J.W., and Moat A.G. Nicotinamide adenine dinucleotide biosynthesis and pyridine nucleotide cycle metabolism in microbial systems. Microbiol. Rev. 44 (1980) 83-105
4. Gerdes S.Y., Scholle M.D., D'Souza M., Bernal A., Baev M.V., Farrell M., Kurnasov O.V., Daugherty M.D., Mseeh F., Polanuyer B.M., Campbell J.W., Anantha S., Shatalin K.Y., Chowdhury S.A., Fonstein M.Y., and Osterman A.L. From genetic footprinting to antimicrobial drug targets: examples in cofactor biosynthetic pathways. J. Bacteriol. 184 (2002) 4555-4572
5. Rizzi M., and Schindelin H. Structural biology of enzymes involved in NAD and molybdenum cofactor biosynthesis. Curr. Opin. Struct. Biol. 12 (2002) 709-720
6. Mattevi A., Tedeschi G., Bacchella L., Coda A., Negri A., and Ronchi S. Structure of l-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family. Structure 7 (1999) 745-756
7. Bossi R.T., Negri A., Tedeschi G., and Mattevi A. Structure of FAD-bound l-aspartate oxidase: insight into substrate specificity and catalysis. Biochemistry 41 (2002) 3018-3024
8. Stetter K.O., Fiala G., Huber G., Huber R., and Segerer A. Hyperthermophilic microorganisms. FEMS Microbiol. Lett. 75 (1990) 117-124
9. Adams M.W.W. Enzymes and proteins from organisms that grow near and above 100 °C. Annu. Rev. Microbiol. 47 (1993) 627-658
10. Woese C.R., Kandler O., and Wheelis M.L. Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya. Proc. Natl. Acad. Sci. 87 (1990) 4576-4579
11. Sakuraba H., Satomura T., Kawakami R., Yamamoto S., Kawarabayasi Y., Kikuchi H., and Ohshima T. l-Aspartate oxidase is present in the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii OT-3: characteristics and role in the de novo biosynthesis of nicotinamide adenine dinucleotide proposed by genome sequencing. Extremophiles 6 (2002) 275-281
12. Yoneda K., Kawakami R., Tagashira Y., Sakuraba H., Goda S., and Ohshima T. The first archaeal l-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: gene cloning and enzymological characterization. Biochim. Biophys. Acta 1764 (2006) 1087-1093
13. Sakuraba H., Kanai K., Goda S., Kawarabayasi Y., and Ohshima T. A nicotinamide mononucleotide adenylyltransferase with unique adenylyl group donor specificity from a hyperthermophilic archaeon, Pyrococcus horikoshii OT3. J. Mol. Catal. B Enzym. 23 (2003) 273-279
14. Sakuraba H., Tsuge H., Yoneda K., Katunuma N., and Ohshima T. Crystal structure of the NAD biosynthetic enzyme quinolinate synthase. J. Biol. Chem. 280 (2005) 26645-26648
15. Yoneda K., Sakuraba H., Tsuge H., Katunuma N., and Ohshima T. Crystal structure of archaeal highly thermostable l-aspartate dehydrogenase-NAD-citrate ternary complex. FEBS Journal 274 (2007) 4315-4325
16. Mortarino M., Negri A., Tedeschi G., Simonic T., Duga S., Gassen H.G., and Ronchi S. l-Aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition. Eur. J. Biochem. 239 (1996) 418-426
17. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
18. Laemmli U.K. Cleavage of structural proteins during the assembly of the bacteriophase T4. Nature 227 (1970) 680-685
19. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
20. Terwilliger T.C., and Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr. 55 (1999) 849-861
21. Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallogr. D 56 (2000) 965-972
22. McRee D.E. XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
23. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. 53 (1997) 240-255
24. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., and Warren G.L. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54 (1998) 905-921
25. Rodriguez R., Chinea G., Lopez N., Pons T., and Vriend G. Homology modeling, model and software evaluation: three related resources. Bioinformatics 14 (1998) 523-528
26. Barlow D.J., and Thornton J.M. Ion-pairs in proteins. J. Mol. Biol. 168 (1983) 867-885
27. Nicholls A., Sharp K.A., and Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11 (1991) 281-296
28. Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
29. Tedeschi G., Negri A., Ceciliani F., Mattevi A., and Ronchi S. Structural characterization of l-aspartate oxidase and identification of an interdomain loop by limited proteolysis. Eur. J. Biochem. 260 (1999) 896-903
30. Chan M.K., Mukund S., Kletzin A., Adams M.W., and Rees D.C. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267 (1995) 1463-1469
31. Yip K.S., Stillman T.J., Britton K.L., Artymiuk P.J., Baker P.J., Sedelnikova S.E., Engel P.C., Pasquo A., Chiaraluce R., and Consalvi V. The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure 3 (1995) 1147-1158
32. Hennig M., Darimont B., Sterner R., Kirschner K., and Jansonius J.N. 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Structure 3 (1995) 1295-1306
33. Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structure. J. Appl. Crystallogr. 26 (1993) 283-291