Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: A potential TB drug target

Structure

Volumn 6, Issue 12, 1998, Pages 1587-1599

  Sharma, Vivek ^a   Grubmeyer, Charles ^b   Sacchettini, James C ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

^b TEMPLE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

NAD biosynthesis; Phosphoribosyltransferase; PRPP; QAPRTase; Quinolinate

Indexed keywords

BACTERIA (MICROORGANISMS); MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS;

EID: 0032534756     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00156-7     Document Type: Article

References (36)

1. Foster, J.W. & Moat, A.G. (1980). Nicotinamide adenine dinucleotide biosynthesis and pyridine nucleotide cycle metabolism in microbial systems. Microbiol. Rev. 44, 83-105.
2. Tritz, G.J. (1987). NAD biosynthesis and recycling. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, Vol. 1. (Neidhart, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M. & Umbarger, H.E., eds), pp. 557-563, American Society for Microbiology, Washington DC, USA.
3. Cole, S.T., et al., & Barrell, B.G. (1998). Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393, 537-544.
4. Foster, J.W., Park., Y.K., Penfound, T., Fenger, T. & Spector, M.P. (1990). Regulation of NAD metabolism in Salmonella typhimurium: molecular sequence analysis of the bifunctional nadR regulator and the nadA-pnuC operon. J. Bacteriol. 172, 4187-4196.
5. Foster, J.W., Kinney, D.M. & Moat, A.G. (1979). Pyridine nucleotide cycle of Salmonella typhimurium: isolation and characterization of pncA, pncB and pncC mutants and utilization of exogenous nicotinamide adenine dinucleotide. J. Bacteriol. 137, 1165-1175.
6. Penfound, T. & Foster, J.W. (1995). Biosynthesis and recycling of NAD. In Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, Vol. 1. (Neidhart, F.C., Ingraham, J.L., Low, K.B., Magasanik, B., Schaechter, M. & Umbarger, H.E., eds), pp. 721-730, American Society for Microbiology, Washington DC, USA.
7. Kallikin, L. & Calvo, K. (1988). Inhibition of quinolinate phosphoribosyltransferase by pyridine analogs of quinolinic acid. Biochem. Biophys. Res. Commun. 152, 559-564.
8. Rozwarski, D.A., Grant, G.A., Barton, D.H.R., Jacobs, W.R. Jr. & Sacchettini, J.C. (1998). Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis. Science 279, 98-102.
9. Meisel, L., Weisbrod, T.R., Marcinkeviciene, J.A., Bittman, R. & Jacobs, W.R.Jr. (1998). NADH dehydrogenase defects confer isoniazid resistance and conditional lethality in Mycobacterium smegmatis. J. Bacteriol. 180, 2459-2467.
10. Scapin, G., Oztruk, D.H., Grubmeyer, C. & Sacchettini, J.C. (1995). The crystal structure of the orotate phosphoribosyltransferase complexed with orotate and alpha-D-5-phosphoribosyl-1-pyrophosphate. Biochemistry 34, 10744-10754.
11. Tao, W., Grubmeyer, C. & Blanchard, J.S. (1996). Transition state structure of Salmonella typhimurium orotate phosphoribosyltransferase. Biochemistry 35, 14-21.
12. Eads, J.C., Scapin, G., Xu, Y., Grubmeyer, C. & Sacchettini, J.C. (1994). The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell 78, 325-331.
13. Smith, J.L., et al., Satow, Y. (1994). Structure of the allosteric regulatory enzyme for purine biosynthesis. Science 264, 1427-1433.
14. Vos, S., de Jersey, J. & Martin, J.L. (1997). Crystal structure of Escherichia coli xanthine phosphoribosyltransferase. Biochemistry 36, 4125-4134.
15. Schumacher, M.A., Carter, D., Ross, D.S., Ullman, B. & Brennan, R.G. (1996). Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop. Nat. Struct. Biol. 3, 881-887.
16. Somoza, J.R., Chin, M.S., Focia, P.J., Wang, C.C. & Fletterick, R.J. (1996). Crystal structure of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from the protozoan parasite Tritrichomonas foetus. Biochemistry 35, 7032-7040.
17. Schumacher, M.A., Carter, D., Scott, D.M., Roos, D.S., Ullman, B. & Brennan, R.G. (1998). Crystal structures of Toxoplasma gondii uracil phosphoribosyltransferase reveal the atomic basis of pyrimidine discrimination and prodrug binding. EMBO J. 17, 3219-3232.
18. Tomchick, D.R., Turner, R.J., Switzer, R.L. & Smith J.L. (1998). Adaptation of an enzyme to regulatory function: structure of Bacillus subtilis PyrR, a pyr RNA-binding attenuation protein and uracil phosphoribosyltransferase. Structure 6, 337-350.
19. Eads, J.C., Oztruk, D., Wexler, T.B., Grubmeyer, C. & Sacchettini, J.C. (1997). A new function for a common fold: the crystal structure of quinolinic acid phosphoribosyltransferase. Structure 5, 47-58.
20. Krahn, J.M., Kim, J.H., Burns, M.R., Parry, R.J., Zalkin, H. & Smith, J.L. (1997). Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site. Biochemistry 36, 11061-11068.
21. Iwai, K. & Taguchi, H. (1974). Purification and crystallization of quinolinate phosphoribosyltransferase from hog liver. Biochem. Biophys. Res. Commun. 56, 884-891.
22. Okuno, E. & Schwarcz, R. (1985). Purification of quinolinic acid phosphoribosyltransferase from rat liver and brain. Biochim. Biophys. Acta 841, 112-119.
23. Okuno, E., White, R.J. & Schwarcz, R.J. (1988). Quinolinic acid phosphoribosyltransferase: purification and partial characterization from human liver and brain. J. Biochem. (Tokyo) 103, 1054-1059.
24. Bhatia, R. & Calvo, K.C. (1996). The sequencing, expression, purification and steady-state kinetic analysis of quinolinate phoshphoribosyltransferase from Escherichia coli. Arch. Bioch. Biophys. 2, 270-278.
25. McClaud, R.W., Fischer, A.C., Mauldin, S.K. & Jones, M.E. (1984). 5-Phosphorylribose-α-methylene bisphosphate: properties of a substrate analog of 5-phosphorylribose 1-α-diphosphate. Biorg. Chem. 12, 339-348.
26. Jencks, W.P. (1997). From chemistry to biochemistry to catalysis to movement. Annu. Rev. Biochem. 66, 1-18.
27. Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend: Data Collection and Processing. (Sawyer, L., Issacs, N. & Bailey, S. eds), pp. 56-62, SERC Daresbury Laboratory, Warrington, UK.
28. Furey, W. & Swaminathan, S. (1990). PHASES - a program package for processing and analysis of diffraction data for macromolecules. Acta Cryst. 18, 73.
29. Jones, T.A. & Kjeldgaard, M. (1993). O Version 5.9.
30. Brünger, A.T. (1992). X-PLOR, Version 3.1. A System for X-ray Crystallography and NMR. Yale University press, New Haven, CT, USA.
31. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 21, 279-281.
32. Collaborative Computational Project No. 4 (1994). The CCP4 suite: programs for crystallography. Acta Cryst. D 50, 760-763.
33. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
34. Merrit, E. & Murphy, M. (1994). RASTER3D Version 2.0: a program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.
35. Thompson, J.D., Higgins, D.G. & Gibson, T.J. (1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
36. Evans, S.V. (1993). SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11, 134-138.