Solution structure of the guanine nucleotide-binding STAS domain of SLC26-related SulP protein Rv1739c from Mycobacterium tuberculosis

Journal of Biological Chemistry

Volumn 286, Issue 10, 2011, Pages 8534-8544

  Sharma, Alok K ^a   Ye, Liwen ^a   Baer, Christina E ^b   Shanmugasundaram, Kumaran ^a   Alber, Tom ^b   Alper, Seth L ^a   Rigby, Alan C ^a,c,d  

^a HARVARD MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c ELI LILLY AND COMPANY   (United States)

^d RN 231 ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL CHANGE; DOCKING CALCULATIONS; GUANINE NUCLEOTIDE-BINDING PROTEINS; GUANINE NUCLEOTIDES; HETERONUCLEAR; IN-SILICO; IN-VITRO; INTRINSIC ACTIVITIES; MULTIDIMENSIONAL NMR; MYCOBACTERIAL; MYCOBACTERIUM TUBERCULOSIS; NMR CHEMICAL SHIFT PERTURBATIONS; NUCLEOTIDE BINDING; PHOTOAFFINITY LABELING; PHYSIOLOGICAL CONCENTRATIONS; ROOT MEAN SQUARE DEVIATIONS; SOLUTION STRUCTURES;

CHEMICAL ANALYSIS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHORYLATION; POSITIVE IONS;

NUCLEOTIDES;

CARRIER PROTEIN; GUANINE NUCLEOTIDE; GUANINE NUCLEOTIDE BINDING PROTEIN; PERMEASE; SOLUTE CARRIER FAMILY 26; SULFATE PERMEASE; SULFATE TRANSPORTER AND ANTISIGMA FACTOR ANTAGONIST; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BETA SHEET; COMPUTER MODEL; CONFORMATIONAL TRANSITION; FLUORESCENCE ANALYSIS; IN VITRO STUDY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PHOTOAFFINITY LABELING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SIGNAL TRANSDUCTION;

ANION TRANSPORT PROTEINS; BACTERIAL PROTEINS; COMPUTER SIMULATION; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP;

MYCOBACTERIUM TUBERCULOSIS;

EID: 79953159884     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.165449     Document Type: Article

References (63)

1. Sherman, T., Chernova, M. N., Clark, J. S., Jiang, L., Alper, S. L., and Nehrke, K. (2005) Am. J. Physiol. Cell Physiol. 289, C341-C351
2. Felce, J., and Saier, M. H., Jr. (2004) J. Mol. Microbiol. Biotechnol. 8, 169-176
3. Dorwart, M. R., Shcheynikov, N., Yang, D., and Muallem, S. (2008) Physiology 23, 104-114
4. Hästbacka, J., de la Chapelle, A., Mahtani, M. M., Clines, G., Reeve-Daly, M. P., Daly, M., Hamilton, B. A., Kusumi, K., Trivedi, B., and Weaver, A. (1994) Cell 78, 1073-1087
5. Höglund, P., Haila, S., Socha, J., Tomaszewski, L., Saarialho-Kere, U., Karjalainen-Lindsberg, M. L., Airola, K., Holmberg, C., de la Chapelle, A., and Kere, J. (1996) Nat. Genet. 14, 316-319
6. Everett, L. A., Glaser, B., Beck, J. C., Idol, J. R., Buchs, A., Heyman, M., Adawi, F., Hazani, E., Nassir, E., Baxevanis, A. D., Sheffield, V. C., and Green, E. D. (1997) Nat. Genet. 17, 411-422
7. Liu, X. Z., Ouyang, X. M., Xia, X. J., Zheng, J., Pandya, A., Li, F., Du, L. L., Welch, K. O., Petit, C., Smith, R. J., Webb, B. T., Yan, D., Arnos, K. S., Corey, D., Dallos, P., Nance, W. E., and Chen, Z. Y. (2003) Hum. Mol. Genet. 12, 1155-1162
8. Jiang, Z., Asplin, J. R., Evan, A. P., Rajendran, V. M., Velazquez, H., Nottoli, T. P., Binder, H. J., and Aronson, P. S. (2006) Nat. Genet. 38, 474-478
9. Dawson, P. A., Russell, C. S., Lee, S., McLeay, S. C., van Dongen, J. M., Cowley, D. M., Clarke, L. A., and Markovich, D. (2010) J. Clin. Invest. 120, 706-712
10. Xu, J., Song, P., Nakamura, S., Miller, M., Barone, S., Alper, S. L., Riederer, B., Bonhagen, J., Arend, L. J., Amlal, H., Seidler, U., and Soleimani, M. (2009) J. Biol. Chem. 284, 29470-29479
11. Xu, J., Song, P., Miller, M. L., Borgese, F., Barone, S., Riederer, B., Wang, Z., Alper, S. L., Forte, J. G., Shull, G. E., Ehrenfeld, J., Seidler, U., and Soleimani, M. (2008) Proc. Natl. Acad. Sci. U.S.A. 105, 17955-17960
12. Tuo, B., Riederer, B., Wang, Z., Colledge, W. H., Soleimani, M., and Seidler, U. (2006) Gastroenterology 130, 349-358
13. Wang, Y., Soyombo, A. A., Shcheynikov, N., Zeng, W., Dorwart, M., Marino, C. R., Thomas, P. J., and Muallem, S. (2006) EMBO J. 25, 5049-5057
14. Ishiguro, H., Namkung, W., Yamamoto, A., Wang, Z., Worrell, R. T., Xu, J., Lee, M. G., and Soleimani, M. (2007) Am. J. Physiol. Gastrointest. Liver Physiol. 292, G447-455
15. Zolotarev, A. S., Unnikrishnan, M., Shmukler, B. E., Clark, J. S., Vandorpe, D. H., Grigorieff, N., Rubin, E. J., and Alper, S. L. (2008) Comp. Biochem. Physiol. A Mol. Integr. Physiol. 149, 255-266
16. Price, G. D., Woodger, F. J., Badger, M. R., Howitt, S. M., and Tucker, L. (2004) Proc. Natl. Acad. Sci. U.S.A. 101, 18228-18233
17. Shelden, M. C., Howitt, S. M., and Price, G. D. (2010) Mol. Membr. Biol. 27, 12-23
18. Babu, M., Greenblatt, J. F., Emili, A., Strynadka, N. C., Reithmeier, R. A., and Moraes, T. F. (2010) Structure 18, 1450-1462
19. Aravind, L., and Koonin, E. V. (2000) Curr. Biol. 10, R53-55
20. Clarkson, J., Campbell, I. D., and Yudkin, M. D. (2003) Biochem. J. 372, 113-119
21. Masuda, S., Murakami, K. S., Wang, S., Anders Olson, C., Donigian, J., Leon, F., Darst, S. A., and Campbell, E. A. (2004) J. Mol. Biol. 340, 941-956
22. Najafi, S. M., Harris, D. A., and Yudkin, M. D. (1996) J. Bacteriol. 178, 6632-6634
23. Kuo, S., Demeler, B., and Haldenwang, W. G. (2008) J. Bacteriol. 190, 6625-6635
24. Kovacs, H., Comfort, D., Lord, M., Campbell, I. D., and Yudkin, M. D. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 5067-5071
25. Seavers, P. R., Lewis, R. J., Brannigan, J. A., Verschueren, K. H., Murshudov, G. N., and Wilkinson, A. J. (2001) Structure 9, 605-614
26. Etezady-Esfarjani, T., Placzek, W. J., Herrmann, T., and Wüthrich, K. (2006) Magn. Reson. Chem. 44, S61-70
27. Serrano, P., Pedrini, B., Geralt, M., Jaudzems, K., Mohanty, B., Horst, R., Herrmann, T., Elsliger, M. A., Wilson, I. A., and Wüthrich, K. (2010) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 1393-1405
28. Quin, M., Newman, J., Firbank, S., Lewis, R. J., and Marles-Wright, J. (2008) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64, 196-199
29. Dorwart, M. R., Shcheynikov, N., Baker, J. M., Forman-Kay, J. D., Muallem, S., and Thomas, P. J. (2008) J. Biol. Chem. 283, 8711-8722
30. Sharma, A. K., Ye, L., Zolotarev, A. S., Alper, S. L., and Rigby, A. C. (2009) Biomol. NMR Assign. 3, 99-102
31. Pasqualetto, E., Aiello, R., Gesiot, L., Bonetto, G., Bellanda, M., and Battistutta, R. (2010) J. Mol. Biol. 400, 448-462
32. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) J. Biomol. NMR 6, 277-293
33. Kraulis, P. J., Domaille, P. J., Campbell-Burk, S. L., Van Aken, T., and Laue, E. D. (1994) Biochemistry 33, 3515-3531
34. Cavanagh, J., Fairbrother, W. J., Palmer, A. G., and Skelton, N. J. (1996) Protein NMR Spectroscopy: Principles and Practice, Academic Press Inc., San Diego, CA
35. Bax, A., and Grzesiek, S. (1993) Acc. Chem. Res. 26, 131-138
36. Muhandiram, D. R., Farrow, N. A., Xu, G. Y., Smallcombe, S., and Kay, L. E. (1993) J. Magn. Reson. Ser. B 102, 317-321
37. Güntert, P., Mumenthaler, C., and Wüthrich, K. (1997) J. Mol. Biol. 273, 283-298
38. Cornilescu, G., Delaglio, F., and Bax, A. (1999) J. Biomol. NMR 13, 289-302
39. Sharma, A. K., Sharma, S. K., Surolia, A., Surolia, N., and Sarma, S. P. (2006) Biochemistry 45, 6904-6916
40. Linge, J. P., Williams, M. A., Spronk, C. A., Bonvin, A. M., and Nilges, M. (2003) Proteins 50, 496-506
41. Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) J. Biomol. NMR 8, 477-486
42. Koradi, R., Billeter, M., and Wuthrich, K. (1996) J. Mol. Graph. 14, 51-55, 29-32
43. Humphrey, W., Dalke, A., and Schulten, K. (1996) J. Mol. Graph. 14, 33-38, 27-28
44. Trott, O., and Olson, A. J. (2010) J. Comput. Chem. 31, 455-461
45. Rao, A., Martin, P., Reithmeier, R. A., and Cantley, L. C. (1979) Biochemistry 18, 4505-4516
46. Greenstein, A. E., MacGurn, J. A., Baer, C. E., Falick, A. M., Cox, J. S., and Alber, T. (2007) PLoS Pathog. 3, e49
47. Buttani, V., Losi, A., Polverini, E., and Gärtner, W. (2006) FEBS Lett. 580, 3818-3822
48. Tang, Y., Cao, Z., Livoti, E., Krauss, U., Jaeger, K. E., Gärtner, W., and Losi, A. (2010) Photochem. Photobiol. Sci. 9, 47-56
49. Mazhab-Jafari, M. T., Marshall, C. B., Smith, M., Gasmi-Seabrook, G. M., Stambolic, V., Rottapel, R., Neel, B. G., and Ikura, M. (2010) J. Biol. Chem. 285, 5132-5136
50. Avila-Pérez, M., Vreede, J., Tang, Y., Bende, O., Losi, A., Gärtner, W., and Hellingwerf, K. (2009) J. Biol. Chem. 284, 24958-24964
51. Bergbrede, T., Chuky, N., Schoebel, S., Blankenfeldt, W., Geyer, M., Fuchs, E., Goody, R. S., Barr, F., and Alexandrov, K. (2009) J. Biol. Chem. 284, 2628-2635
52. Bergbrede, T., Pylypenko, O., Rak, A., and Alexandrov, K. (2005) J. Struct. Biol. 152, 235-238
53. Chang, M. H., Plata, C., Sindic, A., Ranatunga, W. K., Chen, A. P., Zandi-Nejad, K., Chan, K. W., Thompson, J., Mount, D. B., and Romero, M. F. (2009) J. Biol. Chem. 284, 28306-28318
54. Alvarez, B. V., Vilas, G. L., and Casey, J. R. (2005) EMBO J. 24, 2499-2511
55. Hassan, H. A., Mentone, S., Karniski, L. P., Rajendran, V. M., and Aronson, P. S. (2007) Am. J. Physiol. Cell Physiol. 292, C1485-1492
56. Wooff, E., Michell, S. L., Gordon, S. V., Chambers, M. A., Bardarov, S., Jacobs, W. R., Jr., Hewinson, R. G., and Wheeler, P. R. (2002) Mol. Microbiol 43, 653-663
57. Niederweis, M. (2008) Microbiology 154, 679-692
58. Murphy, D. J., and Brown, J. R. (2007) BMC Infect. Dis. 7, 84
59. Riordan, J. T., Tietjen, J. A., Walsh, C. W., Gustafson, J. E., and Whittam, T. S. (2010) Microbiology 156, 719-730
60. Liu, A., Tran, L., Becket, E., Lee, K., Chinn, L., Park, E., Tran, K., and Miller, J. H. (2010) Antimicrob. Agents Chemother. 54, 1393-1403
61. Dong, T., and Schellhorn, H. E. (2009) BMC Genomics 10, 349
62. Byers, D. M., and Gong, H. (2007) Biochem. Cell Biol. 85, 649-662
63. Shibagaki, N., and Grossman, A. R. (2010) J. Biol. Chem. 285, 25094-25102