Structure of the Bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 Å resolution: ATP binding over a barrel

Biochemistry

Volumn 37, Issue 18, 1998, Pages 6247-6255

  Larsen, Todd M ^b   Benning, Matthew M ^b   Rayment, Ivan ^b   Reed, George H ^a  

^a UNIVERSITY OF WISCONSIN   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; MAGNESIUM ION; OXALIC ACID DERIVATIVE; PYRUVATE KINASE; MAGNESIUM; MANGANESE; OXALIC ACID; POTASSIUM; SODIUM;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBUNIT; MUSCLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; RABBIT; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ELECTRON SPIN RESONANCE; ENZYMOLOGY; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ADENOSINE TRIPHOSPHATE; ANIMALS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ELECTRON SPIN RESONANCE SPECTROSCOPY; MAGNESIUM; MANGANESE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUSCLES; OXALATES; OXALIC ACID; POTASSIUM; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PYRUVATE KINASE; RABBITS; SODIUM;

EID: 0032485628     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi980243s     Document Type: Article

References (46)

1. Seeholzer, S. H., Jaworowski, A., and Rose, I. A. (1991) Biochemistry 30, 727-732.
2. Rose, I. A. (1970) J. Biol. Chem. 245, 6052-6056.
3. Rose, I. A. (1960) J. Biol. Chem. 235, 1170-1177.
4. McQuate, J. T., and Utter, M. F. (1959) J. Biol. Chem. 234, 2151-2157.
5. Giles, I. G., Poat, P. C., and Munday, K. A. (1975) Biochem. Soc. Trans. 3, 312-314.
6. Dougherty, T. M., and Cleland, W. W. (1985) Biochemistry 24, 5875-5880.
7. Gallo, A. A., and Sable, H. Z. (1973) Biochim. Biophys. Acta 302, 443-456.
8. Tietz, A., and Ochoa, S. (1958) Arch. Biochem. Biophys. 78, 477-493.
9. Lodato, D. T., and Reed, G. H. (1987) Biochemistry 26, 2243-2250.
10. Reed, G. H., and Morgan, S. D. (1974) Biochemistry 13, 3537-3541.
11. Buchbinder, J. L., and Reed, G. H. (1990) Biochemistry 29, 1799-1806.
12. Buchbinder, J. L., Baraniak, J., Frey, P. A., and Reed, G. H. (1993) Biochemistry 32, 14111-14116.
13. Kofron, J. L., and Reed, G. H. (1990) Arch. Biochem. Biophys. 280, 40-44.
14. Muirhead, H., Clayden, D. A., Barford, D., Lorimer, C. G., Fothergill-Gilmore, L. A., and Schmitt, W. (1986) EMBO J. 5, 475-481.
15. Larsen, T. M., Laughlin, L. T., Holden, H. M., Rayment, I., and Reed, G. H. (1994) Biochemistry 33, 6301-6309.
16. Larsen, T. M., Benning, M. M., Wesenberg, G. E., Rayment, I., and Reed, G. H. (1997) Arch. Biochem. Biophys. 345, 199-206.
17. Walker, J. E., Saraste, M., Runswick, J. M., and Gay, N. J. (1982) EMBO J. 1, 945-951.
18. Milner-White, E. J., Coggins, J. R., and Anton, I. A. (1991) J. Mol. Biol. 221, 751-754.
19. Teng, T.-Y. (1994) J. Appl. Crystallogr. 23, 387-391.
20. Rodgers, D. W. (1997) Methods Enzymol. 276, 183-203.
21. Navaza, J. (1987) Acta Crystallogr. A43, 645-653.
22. Navaza, J. (1990) Acta Crystallogr. A46, 619-620.
23. Tronrud, D. E., Ten Eyck, L. F., and Matthews, B. W. (1987) Acta Crystallogr. A43, 489-501.
24. Jones, T. A. (1985) Methods Enzymol. 115, 157-171.
25. Jones, T. A., Zou, J.-Y., Cowan, S. W., and Kjeldguard, M. (1991) Acta Crystallogr. A47, 110-119.
26. Lu, A., Shorter, A. L., and Dunaway-Mariano, D. (1993) Biochemistry 32, 2378-2385.
27. Jaffe, E. K. (1979) Ph.D. Dissertation, University of Pennsylvania, Philadelphia, PA.
28. Kayne, F. J. (1973) Enzymes (3rd Ed.) 8, 353-382.
29. Bezares, G., Eyzaguirre, J., Hinrichs, M. V., Heinrikson, R. L., Reardon, I., Kemp, R. G., Latshaw, S. P., and Bazaes, S. (1987) Arch. Biochem. Biophys. 253, 133-137.
30. Kobayashi, N., and Go, N. (1997) Nat. Struct. Biol. 4, 6-7.
31. Tari, L. W., Matte, A., Pugazhenthi, U., Goldie, H., & Belbaere, L. T. J. (1996) Nat. Struct. Biol. 3, 355-363.
32. Tari, L. W., Matte, A., Goldie, H., & Delbaere, L. T. J. (1997) Nat. Struct. Biol. 4, 990-994.
33. Kayne, F. J. (1971) Arch. Biochem. Biophys. 143, 232-239.
34. Blättler, W. A., and Knowles, J. R. (1979) Biochemistry 18, 3927-3933.
35. Knowles, J. R. (1980) Annu. Rev. Biochem. 49, 877-919.
36. Reed, G. H., and Cohn, M. (1973) J. Biol. Chem. 248, 6436-6442.
37. Robinson, J. L., and Rose, I. A. (1972) J. Biol. Chem. 247, 1096-1105.
38. Gupta, R. K., Oesterling, R. M., and Mildvan, A. S. (1976) Biochemistry 15, 2881-2887.
39. Gupta, R. K., and Mildvan, A. S. (1977) J. Biol. Chem. 252, 5967-5976.
40. Cornelius, R. D., Hart, P. A., and Cleland, W. W. (1977) Inorg. Chem. 16, 2799-2805.
41. Block, H., and Gold, V. (1959) J. Chem. Soc., 966-975.
42. Rose, I. A., and Kuo, D. J. (1989) Biochemistry 28, 9579-9585.
43. Rose, I. A., Kuo, D. J., and Warms, J. V. B. (1991) Biochemistry 30, 722-726.
44. Bai, Y., Milne, J. S., Mayne, L., and Englander, S. W. (1993) Proteins: Struct., Funct., Genet. 17, 75-86.
45. Laskowski, R. A., MacArthur, M. W., Moss, S. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291.
46. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950.