Structural Basis for the Aldolase and Epimerase Activities of Staphylococcus aureus Dihydroneopterin Aldolase

Journal of Molecular Biology

Volumn 368, Issue 1, 2007, Pages 161-169

  Blaszczyk, Jaroslaw ^a,b   Li, Yue ^b   Gan, Jianhua ^a   Yan, Honggao ^b   Ji, Xinhua ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b Michigan State University   (United States)

Author keywords

aldolase; dihydromonapterin; dihydroneopterin; dihydroneopterin aldolase; pterin

Indexed keywords

EPIMERASE; FRUCTOSE BISPHOSPHATE ALDOLASE; NEOPTERIN; PHORBOL DIBUTYRATE; PTERIN DERIVATIVE;

ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; EPIMERIZATION; MOLECULAR MECHANICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; REACTION ANALYSIS; STAPHYLOCOCCUS AUREUS;

STAPHYLOCOCCUS AUREUS;

EID: 33947301270     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.02.009     Document Type: Article

References (22)

1. Blakley R.L., and Benkovic S.J. Chemistry and biochemistry of folates. In: Blakley R.L., and Benkovic S.J. (Eds). Folates and Pterins vol. 1 (1984), John Wiley and Sons, Inc., New York
2. In: O'Grady F., Lambert H.P., Finch R.G., and Greenwood D. (Eds). Antibiotic and Chemotherapy: Anti-Infective Agents and Their Use in Therapy. 7th edit. (1997), Churchill Livingstone, Churchill Livingstone, New York
3. Haußmann C., Rohdich F., Schmidt E., Bacher A., and Richter G. Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase. J. Biol. Chem. 273 (1998) 17418-17424
4. Mathis J.B., and Brown G.M. The biosynthesis of folic acid. XI. Purification and properties of dihydroneopterin aldolase. J. Biol. Chem. 245 (1970) 3015-3025
5. Luo Y., Samuel J., Mosimann S.C., Lee J.E., Tanner M.E., and Strynadka N.C. The structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like platform for epimerization. Biochemistry 40 (2001) 14763-14771
6. Hennig M., D'Arcy A., Hampele I.C., Page M.G., Oefner C., and Dale G.E. Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus. Nat. Struct. Biol. 5 (1998) 357-362
7. Sanders W.J., Nienaber V.L., Lerner C.G., McCall J.O., Merrick S.M., Swanson S.J., et al. Discovery of potent inhibitors of dihydroneopterin aldolase using CrystaLEAD high-throughput X-ray crystallographic screening and structure-directed lead optimization. J. Med. Chem. 47 (2004) 1709-1718
8. Bauer S., Schott A.K., Illarionova V., Bacher A., Huber R., and Fischer M. Biosynthesis of tetrahydrofolate in plants: crystal structure of 7,8-dihydroneopterin aldolase from Arabidopsis thaliana reveals a novel aldolase class. J. Mol. Biol. 339 (2004) 967-979
9. Goulding C.W., Apostol M.I., Sawaya M.R., Phillips M., Parseghian A., and Eisenberg D. Regulation by oligomerization in a mycobacterial folate biosynthetic enzyme. J. Mol. Biol. 349 (2005) 61-72
10. Garcon A., Levy C., and Derrick J.P. Crystal structure of the bifunctional dihydroneopterin aldolase/6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Streptococcus pneumoniae. J. Mol. Biol. 360 (2006) 644-653
11. Wang Y., Li Y., and Yan H. Mechanism of dihydroneopterin aldolase: functional functional roles of the conserved active site glutamate and lysine residues. Biochemistry 45 (2006) 15232-15239
12. Wang Y., Scherperel G., Roberts K.D., Jones A.D., Reid G.E., and Yan H. A point mutation converts dihydroneopterin aldolase to a cofactor-independent oxygenase. J. Am. Chem. Soc. 128 (2006) 13216-13223
13. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
14. Reed R.J. Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallog. sect. D 5D7 (2000) 1373-1382
15. Storoni L.C., McCoy A.J., and Read R.J. Likelihood-enhanced fast rotation functions. Acta Crystallog. sect. D, Crystallogr. D 60 (2004) 432-438
16. McCoy A.J., Grosse-Kunstleve R.W., Storoni L.C., and Read R.J. Likelihood-enhanced fast translation functions. Acta Crystallog. sect. D 61 (2005) 458-464
17. Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography and NMR system: A a new software suite for macromolecular structure determination. Acta Crystallog. sect. D 54 (1998) 905-921
18. Sheldrick G.M., and Schneider T.R. SHELXL: high-resolution refinement. Methods Enzymol. 277 (1997) 319-343
19. Jones T.A., and Kjeldgaard M. Electron-density map interpretation. Methods Enzymol. 277 (1997) 173-208
20. Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24 (1991) 946-950
21. Esnouf R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15 (1997) 132-134
22. DeLano W.L. The PyMOL Molecular Graphics System (2002), Delano Scientific, San Carlos, CA, USA