Skip to main content
SpringerLink
Log in

NMR assignment and secondary structure of the STAS domain of Rv1739c, a putative sulfate transporter of Mycobacterium tuberculosis

  • Article
  • Published:
Biomolecular NMR Assignments Aims and scope Submit manuscript

Abstract

We report 1HN, 15N, and 13C resonance assignments for the 15.6 kDa STAS domain of the putative sulfate transporter of Mycobacterium tuberculosis, Rv1739c, using heteronuclear, multidimensional NMR spectroscopy. Rv1739c is a SulP anion permease, related in structure to the SLC26 gene family of metazoan anion exchangers and anion channels.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2

Similar content being viewed by others

References

  • Aravind L, Koonin EV (2000) The STAS domain—a link between anion transporters and antisigma-factor antagonists. Curr Biol 10:R53–R55. doi:10.1016/S0960-9822(00)00335-3

    Article  Google Scholar 

  • Berjanskii MV, Wishart DS (2008) Application of the random coil index to studying protein flexibility. J Biomol NMR 40:31–48. doi:10.1007/s10858-007-9208-0

    Article  Google Scholar 

  • Cavanagh J, Fairbrother WJ, Palmer AG et al (1996) Protein NMR spectroscopy: principles and practice. Academic Press, Inc., San Diego, CA

    Google Scholar 

  • Chernova MN, Jiang L, Shmukler BE et al (2003) Acute regulation of the SLC26A3 congenital chloride diarrhoea anion exchanger (DRA) expressed in Xenopus oocytes. J Physiol 549:3–19. doi:10.1113/jphysiol.2003.039818

    Article  Google Scholar 

  • Clarkson J, Campbell ID, Yudkin MD et al (2003) Phosphorylation induces subtle structural changes in SpoIIAA, a key regulator of sporulation. Biochem J 372:113–119. doi:10.1042/BJ20021748

    Article  Google Scholar 

  • Delaglio F, Grzesiek S, Vuister GW et al (1995) NMR pipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293. doi:10.1007/BF00197809

    Article  Google Scholar 

  • Dorwart MR, Shcheynikov N, Baker JM et al (2008a) Congenital chloride-losing diarrhea causing mutations in the STAS domain result in misfolding and mistrafficking of SLC26A3. J Biol Chem 283:8711–8722. doi:10.1074/jbc.M704328200

    Article  Google Scholar 

  • Dorwart MR, Shcheynikov N, Yang D et al (2008b) The solute carrier 26 family of proteins in epithelial ion transport. Physiology (Bethesda) 23:104–114. doi:10.1152/physiol.00037.2007

    Google Scholar 

  • Etezady-Esfarjani T, Placzek WJ, Herrmann T et al (2006) Solution structures of the putative anti-sigma-factor antagonist TM1442 from Thermotoga maritima in the free and phosphorylated states. Magn Reson Chem 44:S61–S70. doi:10.1002/mrc.1831

    Article  Google Scholar 

  • Felce J, Saier MH Jr (2004) Carbonic anhydrases fused to anion transporters of the SulP family: evidence for a novel type of bicarbonate transporter. J Mol Microbiol Biotechnol 8:169–176. doi:10.1159/000085789

    Article  Google Scholar 

  • Kraulis PJ (1989) ANSIG—a program for the assignment of protein 1H 2D-NMR spectra by interactive computer-graphics. J Magn Reson 24:627–633

    Google Scholar 

  • Lee JY, Ahn HJ, Ha KS et al (2004) Crystal structure of the TM1442 protein from Thermotoga maritima, a homolog of the Bacillus subtilis general stress response anti-anti-sigma factor RsbV. Proteins 56:176–179. doi:10.1002/prot.20166

    Article  Google Scholar 

  • Oganesyan N, Kim SH, Kim R (2004) On-column chemical refolding of proteins. Pharmagenomics 4:22–25

    Google Scholar 

  • Seavers PR, Lewis RJ, Brannigan JA et al (2001) Structure of the Bacillus cell fate determinant SpoIIAA in phosphorylated and unphosphorylated forms. Structure 9:605–614. doi:10.1016/S0969-2126(01)00623-2

    Article  Google Scholar 

  • Wishart DS, Sykes BD (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4:171–180. doi:10.1007/BF00175245

    Article  Google Scholar 

  • Zolotarev AS, Unnikrishnan M, Shmukler BE et al (2008) Increased sulfate uptake by E. coli overexpressing the SLC26-related SulP protein Rv1739c from Mycobacterium tuberculosis. Comp Biochem Physiol A Mol Integr Physiol 149:255–266. doi:10.1016/j.cbpa.2007.12.005

    Article  Google Scholar 

Download references

Acknowledgements

All NMR experiments were performed at Tufts University Biological NMR Center. This work was supported by NIH grants DK43495 (SLA), DK34854 (Harvard Digestive Diseases Center to SLA) and in part AI063430 (ACR). LY was supported by NIH training grant T32-DK007199 and AKS was supported by AI063430.

Author information

Authors and Affiliations

  1. Division of Molecular Vascular Medicine, Center for Vascular Biology Research, Beth Israel Deaconess Medical Center, RN-231 99 Brookline Ave, Boston, MA, 02215, USA

    Alok K. Sharma, Liwen Ye, Alexander S. Zolotarev, Seth L. Alper & Alan C. Rigby

  2. Renal Division and Molecular Vascular Medicine Unit RW763, Beth Israel Deaconess Medical Center, 330 Brookline Ave, Boston, 02215, MA, USA

    Liwen Ye, Alexander S. Zolotarev & Seth L. Alper

  3. Department of Medicine, Harvard Medical School, Boston, 02215, MA, USA

    Alok K. Sharma, Liwen Ye, Alexander S. Zolotarev, Seth L. Alper & Alan C. Rigby

Authors
  1. Alok K. Sharma
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Liwen Ye
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Alexander S. Zolotarev
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Seth L. Alper
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Alan C. Rigby
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding authors

Correspondence to Seth L. Alper or Alan C. Rigby.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Sharma, A.K., Ye, L., Zolotarev, A.S. et al. NMR assignment and secondary structure of the STAS domain of Rv1739c, a putative sulfate transporter of Mycobacterium tuberculosis . Biomol NMR Assign 3, 99–102 (2009). https://doi.org/10.1007/s12104-009-9150-z

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12104-009-9150-z

Keywords

Search

Navigation