Divergence in macromolecular assembly: X-ray crystallographic structure analysis of lumazine synthase from Brucella abortus
We have determined the three-dimensional structure of 6,7-dimethyl-8-ribityllumazine synthase (lumazine synthase) from Brucella abortus, the infectious organism of the disease brucellosis in animals. This enzyme catalyses the formation of 6,7-dimethyl-8-ribityllumazine, the penultimate product in th...
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Academic Press
2000
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 08950caa a22008777a 4500 | ||
|---|---|---|---|
| 001 | PAPER-2377 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203146.0 | ||
| 008 | 190411s2000 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0034646571 | |
| 024 | 7 | |2 cas |a riboflavin synthase, 9075-82-5 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a JMOBA | ||
| 100 | 1 | |a Braden, B.C. | |
| 245 | 1 | 0 | |a Divergence in macromolecular assembly: X-ray crystallographic structure analysis of lumazine synthase from Brucella abortus |
| 260 | |b Academic Press |c 2000 | ||
| 270 | 1 | 0 | |m Braden, B.C.; Department of Natural Sciences, Bowie State University, Bowie, MD, United States; email: bbraden@bowiestate.edu |
| 506 | |2 openaire |e Política editorial | ||
| 504 | |a Bacher, A., Baur, R., Eggers, U., Harders, H.D., Otto, M.K., Schnepple, H., Riboflavin synthases of Bacillus subtilis. Purification and properties (1980) J. Biol. Chem., 255, pp. 632-637 | ||
| 504 | |a Bacher, A., Ludwig, H.C., Schnepple, H., Ben-Shaul, Y., Heavy riboflavin synthase from Bacillus subtilis. Quaternary structure and reaggregation (1986) J. Mol. Biol., 187, pp. 75-86 | ||
| 504 | |a Brunger, A.T., Adams, P.D., Clore, G.M., Delano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.-S., Warren, G.L., Crystallography and NMR system: A new software system for macromolecular structure determination (1998) Acta Crystallog. Sect. D, 54, pp. 905-921 | ||
| 504 | |a De Mot, R., Nagy, I., Schoofs, G., Vanderleyden, J., Identification of a Rhodococcus gene cluster encoding a homolog of the 17-kDa antigen of Brucella and a putative regulatory protein of the AsnC-Lrp family (1996) Curr. Microbiol., 33, pp. 26-30 | ||
| 504 | |a Garcia-Ramirez, J.J., Santos, M.A., Revuelta, J.L., The Saccharomyces cerevisiae RIB4 gene codes for 6,7-dimethyl-8-ribityllumazine synthase involved in riboflavin biosynthesis. Molecular characterization of the gene and purification of the encoded protein (1995) J. Biol. Chem., 270, pp. 23801-23807 | ||
| 504 | |a Goldbaum, F.A., Polikarpov, I., Cauerhff, A.A., Velikovsky, C.A., Braden, B.C., Poljak, R.J., Crystallization and preliminary X-ray diffraction analysis of the lumazine synthase from Brucella abortus (1998) J. Struct. Biol., 123, pp. 175-178 | ||
| 504 | |a Goldbaum, F.A., Velikovsky, C.A., Baldi, P.C., Mortl, S., Bacher, A., Fossati, C.A., The 18 kDa cytoplasmic protein of Brucella spp. is an enzyme with lumazine synthase activity (1999) J. Med. Microbiol., 48, pp. 833-839 | ||
| 504 | |a Jordan, D.B., Bacot, K.O., Carlson, T.J., Kessel, M., Viitanen, P.V., Plant riboflavin biosynthesis. Cloning, chloroplast location, expression, purification, and partial characterization of spinach lumazine synthase (1999) J. Biol. Chem., 274, pp. 22114-22121 | ||
| 504 | |a Ladenstein, R., Schneider, M., Huber, R., Bartunik, H.D., Wilson, K., Schott, K., Bacher, A., Heavy riboflavin synthase from Bacillus subtilis. Crystal structure analysis of the icosahedral β60 capsid at 3. 3 Å resolution (1988) J. Mol. Biol., 203, pp. 1045-1070 | ||
| 504 | |a Mortl, S., Fischer, M., Richter, G., Tack, J., Weinkauf, S., Bacher, A., Biosynthesis of riboflavin. Lumazine synthase of Escherichia coli (1996) J. Biol. Chem., 271, pp. 33201-33207 | ||
| 504 | |a Otwinowski, Z., Minor, W., Processing of X-ray diffraction data collected in oscillation mode (1997) Methods Enzymol., 276, pp. 307-326 | ||
| 504 | |a Ritsert, K., Huber, R., Turk, D., Ladenstein, R., Schmidt-Base, K., Bacher, A., Studies of the lumazine synthase/riboflavin synthase complex of Bacillus subtilis: Crystal structure analysis of reconstituted, icosahedral β-subunit capsids with bound substrate analogue inhibitor at 2.4 Å resolution (1995) J. Mol. Biol., 253, pp. 151-167 | ||
| 504 | |a Roussel, A., Inisan, A.G., (1992), TURBO-FRODO, Technopole de Chateau-Gombert, Europarc Bat. C. Marseille, France; Staszkiewicz, J., Lewis, C.M., Colville, J., Zervos, M., Band, J., Outbreak of Brucella melitensis among microbiology laboratory workers in a community hospital (1991) J. Clin. Microbiol., 29, pp. 287-290 | ||
| 504 | |a Volk, R., Bacher, A., Biosynthesis of riboflavin. The structure of the 4-carbon precursor (1988) J. Amer. Chem. Soc., 110, pp. 3651-3653 | ||
| 520 | 3 | |a We have determined the three-dimensional structure of 6,7-dimethyl-8-ribityllumazine synthase (lumazine synthase) from Brucella abortus, the infectious organism of the disease brucellosis in animals. This enzyme catalyses the formation of 6,7-dimethyl-8-ribityllumazine, the penultimate product in the synthesis of riboflavin. The three-dimensional X-ray crystal structure of the enzyme from B. abortus has been solved and refined at 2.7 Å resolution to a final R-value of 0.18 (R(free) = 0.23). The macromolecular assembly of the enzyme differs from that of the enzyme from Bacillus subtilis, the only other lumazine synthase structure known. While the protein from B. subtilis assembles into a 60 subunit icosahedral capsid built from 12 pentameric units, the enzyme from B. abortus is pentameric in its crystalline form. Nonetheless, the active sites of the two enzymes are virtually identical indicating inhibitors to theses enzymes could be effective pharmaceuticals across a broad species range. Furthermore, we compare the structures of the enzyme from B. subtilis and B. abortus and describe the C teminus structure which accounts for the differences in quaternary structure. (C) 2000 Academic Press. |l eng | |
| 536 | |a Detalles de la financiación: Universidad de Buenos Aires | ||
| 536 | |a Detalles de la financiación: National Aeronautics and Space Administration, NCC5-232 | ||
| 536 | |a Detalles de la financiación: National Institutes of Health, 1R15AI44790-01 | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas | ||
| 536 | |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas | ||
| 536 | |a Detalles de la financiación: The authors thank Dr Roberto Poljak for critical reading of the manuscript. Additional thanks to Ms Tarice Barnes (Bowie State University) for assistance in the preparation of some lumazine synthase crystals. This work was supported by National Institutes of Health grant 1R15AI44790-01 and National Aeronautics and Space Administration grant NCC5-232 (Model Institutes for Excellence) to B.C.B., C.A.V., A.A.C. and F.A.G. were supported by grants and fellowships from the Consejo Nacional de Investigaciones Cientificas y Técnicas (CONICET), ANPCYT and the University of Buenos Aires. The authors would would like to acknowledge that another lumazine synthase which also assembles in pentameric form has recently been published (Persson et al . (1999) Protein Science , 8 , 2355-2365). | ||
| 593 | |a Department of Natural Sciences, Bowie State University, Bowie, MD, United States | ||
| 593 | |a Facultad De Farmacia Y Bioquímica UBA, Instistuto De Estudios De La Inmunidat Humoral (IDEHU), Buenos Aires, Argentina | ||
| 593 | |a Laborótorio Nacional De Luz Síncrotron, Campinas, SP, Brazil | ||
| 593 | |a Instituto De Investigaciones Bioquímicas, Fundación Campomar, IIBBA-CONICET FCEN-UBA, Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a BRUCELLA ABORTUS |
| 690 | 1 | 0 | |a LUMAZINE SYNTHASE |
| 690 | 1 | 0 | |a MACROMOLECULAR ASSEMBLY |
| 690 | 1 | 0 | |a RIBOFLAVIN SYNTHASE |
| 690 | 1 | 0 | |a X-RAY STRUCTURE ANALYSIS |
| 690 | 1 | 0 | |a BACTERIAL ENZYME |
| 690 | 1 | 0 | |a CAPSID PROTEIN |
| 690 | 1 | 0 | |a LUMAZINE SYNTHASE |
| 690 | 1 | 0 | |a RIBOFLAVIN SYNTHASE |
| 690 | 1 | 0 | |a UNCLASSIFIED DRUG |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a BACILLUS SUBTILIS |
| 690 | 1 | 0 | |a BRUCELLOSIS |
| 690 | 1 | 0 | |a CARBOXY TERMINAL SEQUENCE |
| 690 | 1 | 0 | |a ENZYME STRUCTURE |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a STRUCTURE ANALYSIS |
| 690 | 1 | 0 | |a X RAY CRYSTALLOGRAPHY |
| 690 | 1 | 0 | |a BRUCELLA ABORTUS |
| 700 | 1 | |a Velikovsky, C.A. | |
| 700 | 1 | |a Cauerhff, A.A. | |
| 700 | 1 | |a Polikarpov, I. | |
| 700 | 1 | |a Goldbaum, F.A. | |
| 773 | 0 | |d Academic Press, 2000 |g v. 297 |h pp. 1031-1036 |k n. 5 |p J. Mol. Biol. |x 00222836 |w (AR-BaUEN)CENRE-1757 |t Journal of Molecular Biology | |
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