Monovalent cation dependence and preference of GHKL ATPases and kinases

FEBS Letters

Volumn 544, Issue 1-3, 2003, Pages 268-273

  Hu, Xiaojian ^a   Machius, Mischa ^b   Yang, Wei ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

Active site; Catalysis; GHKL ATPase and kinase; Monovalent cation

Indexed keywords

2 OXOISOVALERATE DEHYDROGENASE (LIPOAMIDE); ADENOSINE TRIPHOSPHATASE; ALANINE; BACTERIAL PROTEIN; DNA TOPOISOMERASE (ATP HYDROLYSING); HEAT SHOCK PROTEIN 90; MAGNESIUM ION; MONOVALENT CATION; POTASSIUM ION; PROLINE; PROTEIN; PROTEIN MUT L; PROTEIN SERINE KINASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; DRUG DESIGN; ENZYMATIC ASSAY; ENZYME ACTIVITY; ENZYME BINDING; GENETIC ANALYSIS; MITOCHONDRIAL MEMBRANE; MOLECULAR MIMICRY; NONHUMAN; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN HYDROLYSIS; PROTEIN MOTIF; PROTEIN TARGETING; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS);

EID: 0038018403     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(03)00519-2     Document Type: Article

References (32)

1. Mushegian A.R., Bassett D.E. Jr., Boguski M.S., Bork P., Koonin E.V. Proc. Natl. Acad. Sci. USA. 94:1997;5831-5836.
2. Dutta R., Inouye M. Trends Biochem. Sci. 25:2000;24-28.
3. Yang, W. (2002) in: Histidine Kinases in Signal Transduction (Masayori Inouye and Rinku Dutta, Eds.), pp. 219-236, Academic Press, New York.
4. Bergerat A., de Massy B., Gadelle D., Varoutas P.-C., Nicolas A., Forterre P. Nature. 386:1997;414-417.
5. Smirnova I.N., Kasho V.N., Faller L.D. FEBS Lett. 431:1998;309-314.
6. Wigley D.B., Davies G.J., Dodson E.J., Maxwell A., Dodson G. Nature. 351:1991;624-629.
7. Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. Cell. 90:1997;65-75.
8. Bilwes A.M., Quezada C.M., Croal L.R., Crane B.R., Simon M.I. Nat. Struct. Biol. 8:2001;353-360.
9. Machius M., Chuang J.L., Wynn R.M., Tomchick D.R., Chuang D.T. Proc. Natl. Acad. Sci. USA. 98:2001;11218-11223.
10. Ban C., Junop M., Yang W. Cell. 97:1999;85-97.
11. Guarne A., Junop M.S., Yang W. EMBO J. 20:2001;5521-5531.
12. Gellert M., O'Dea M.H., Itoh T., Tomizawa J. Proc. Natl. Acad. Sci. USA. 73:1976;4474-4478.
13. Lewis R.J., Singh O.M., Smith C.V., Skarzynski T., Maxwell A., Wonacott A.J., Wigley D.B. EMBO J. 15:1996;1412-1420.
14. Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U., Pavletich N.P. Cell. 89:1997;239-250.
15. Roe S.M., Prodromou C., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. J. Med. Chem. 42:1999;260-266.
16. Ban C., Yang W. Cell. 95:1998;541-552.
17. Marcu M.G., Schulte T.W., Neckers L. J. Natl. Cancer Inst. 92:2000;242-248.
18. Tanaka T., et al. Nature. 396:1998;88-92.
19. Feng G., Winkler M.E. Biotechniques. 19:1995;956-965.
20. Otwinowski Z., Minor W. Methods Enzymol. 276:1997;307-326.
21. Jones T.A., Zou J.-Y., Cowan S.W. Acta Crystallogr. A. 47:1991;110-119.
22. Brünger A.T., et al. Acta Crystallogr. D. 54:1998;905-921.
23. CCP4, 1994. Acta Crystallogr. D 50, 760-763.
24. Nayal M., Di Cera E. J. Mol. Biol. 256:1996;228-234.
25. Obermann W.M., Sondermann H., Russo A.A., Pavletich N.P., Hartl F.U. J. Cell Biol. 143:1998;901-910.
26. Pettit G.R., Moser B.R., Boyd M.R., Schmidt J.M., Pettit R.K., Chapuis J.C. Anticancer Drug Des. 16:2001;185-193.
27. Pettit G.R., Grealish M.P., Jung M.K., Hamel E., Pettit R.K., Chapuis J.C., Schmidt J.M. J. Med. Chem. 45:2002;2534-2542.
28. Conn G.L., Gittis A.G., Lattman E.E., Misra V.K., Draper D.E. J. Mol. Biol. 318:2002;963-973.
29. Nixon P.L., Giedroc D.P. J. Mol. Biol. 296:2000;659-671.
30. Parkinson G.N., Lee M.P., Neidle S. Nature. 417:2002;876-880.
31. Pelletier H., Sawaya M.R., Wolfle W., Wilson S.H., Kraut J. Biochemistry. 35:1996;12742-12761.
32. Wang J.Y., Ling H., Yang W., Craigie R. EMBO J. 20:2001;7333-7343.