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1H, 13C, 15N resonance assignments of the extracellular loop 1 domain (ECL1) of Streptococcus pneumoniae D39 FtsX, an essential cell division protein

Biomolecular NMR Assignments volume 10, pages 89–92 (2016)Cite this article

Abstract

FtsX is an integral membrane protein from Streptococcus pneumoniae (pneumococcus) that harbors an extracellular loop 1 domain (\({\text{FtsX}}^{\text{ECL1}}_{Spn}\)) that interacts with PcsB, an peptidoglycan hydrolase that is essential for cell growth and division. Here, we report nearly complete backbone and side chain resonance assignments and a secondary structural analysis of \({\text{FtsX}}^{\text{ECL1}}_{Spn}\) (residues 47–168 of FtsX) as first steps toward structure determination of \({\text{FtsX}}^{\text{ECL1}}_{Spn}\).

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References

  • Bartual SG, Straume D, Stamsas GA, Munoz IG, Alfonso C, Martinez-Ripoll M, Havarstein LS, Hermoso JA (2014) Structural basis of PcsB-mediated cell separation in Streptococcus pneumoniae. Nat Commun 5:3842

  • Bax A, Clore GM, Gronenborn AM (1990) 1H-1H correlation via isotropic mixing of 13C magnetization, a new three-dimensional approach for assigning 1H and 13C spectra of 13C-enriched proteins. J Magn Reson 88(2):425–431

    ADS  Google Scholar 

  • Delaglio F, Grzesiek S, Vuister G, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277–293

    Article  Google Scholar 

  • Grzesiek S, Anglister J, Bax A (1993) Correlation of backbone amide and aliphatic side-chain resonances in 13C/15N-enriched proteins by isotropic mixing of 13C magnetization. J Magn Reson 101(1):114–119

    Article  Google Scholar 

  • Mavrici D, Marakalala MJ, Holton JM, Prigozhin DM, Gee CL, Zhang YJJ, Rubin EJ, Alber T (2014) Mycobacterium tuberculosis FtsX extracellular domain activates the peptidoglycan hydrolase, RipC. Proc Natl Acad Sci USA 111(22):8037–8042

    Article  ADS  Google Scholar 

  • Montelione GT, Lyons BA, Emerson SD, Tashiro M (1992) An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically-enriched proteins. J Am Chem Soc 114(27):10974–10975

    Article  Google Scholar 

  • Sham LT, Barendt SM, Kopecky KE, Winkler ME (2011) Essential PcsB putative peptidoglycan hydrolase interacts with the essential FtsX(Spn) cell division protein in Streptococcus pneumoniae D39. Proc Natl Acad Sci USA 108(45):E1061–E1069

    Article  ADS  Google Scholar 

  • Sham LT, Jensen KR, Bruce KE, Winkler ME (2013) Involvement of FtsE ATPase and FtsX extracellular loops 1 and 2 in FtsEX-PcsB complex function in cell division of Streptococcus pneumoniae D39. MBio 4(4):e00431-13. doi:10.1128/mBio.00431-13

    Article  Google Scholar 

  • Sheffield P, Garrard S, Derewenda Z (1999) Overcoming expression and purification problems of RhoGDI using a family of “parallel” expression vectors. Protein Expr Purific 15(1):34–39

    Article  Google Scholar 

  • Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS plus : a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44(4):213–223

    Article  Google Scholar 

Download references

Acknowledgments

This work was supported by NIH Grants GM042569 (to D. P. G.), GM114315 (to M. E. W.) and a predoctoral Quantitative and Chemical Biology (QCB) institutional training grant fellowship supported by T32 GM109825 (to B.R.).

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Authors and Affiliations

  1. Department of Chemistry, Indiana University, 212 S. Hawthorne Drive, Bloomington, IN, 47405-7102, USA

    Yue Fu & David P. Giedroc

  2. Department of Biology, Indiana University, Bloomington, IN, 47405, USA

    Kevin E. Bruce, Britta Rued & Malcolm E. Winkler

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  1. Yue Fu
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  2. Kevin E. Bruce
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  3. Britta Rued
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  4. Malcolm E. Winkler
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  5. David P. Giedroc
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Correspondence to David P. Giedroc.

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Fu, Y., Bruce, K.E., Rued, B. et al. 1H, 13C, 15N resonance assignments of the extracellular loop 1 domain (ECL1) of Streptococcus pneumoniae D39 FtsX, an essential cell division protein. Biomol NMR Assign 10, 89–92 (2016). https://doi.org/10.1007/s12104-015-9644-9

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  • DOI: https://doi.org/10.1007/s12104-015-9644-9

Keywords

  • Bacterial cell wall
  • Divisome
  • Peptidoglycan hydrolysis
  • ABC transporter
  • Allostery
  • Extracellular signaling