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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


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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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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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).

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