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. 2016 Apr;10(1):89-92. doi: 10.1007/s12104-015-9644-9. Epub 2015 Sep 14.

Abstract

FtsX is an integral membrane protein from Streptococcus pneumoniae (pneumococcus) that harbors an extracellular loop 1 domain (FtsX(Spn)ECL1) 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 FtsX(Spn)ECL1 (residues 47-168 of FtsX) as first steps toward structure determination of FtsX(Spn)ECL1.

Keywords: ABC transporter; Allostery; Bacterial cell wall; Divisome; Extracellular signaling; Peptidoglycan hydrolysis.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Bacterial Proteins / chemistry*
  • Carbon Isotopes
  • Cell Cycle Proteins / chemistry*
  • Cell Division*
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Domains
  • Streptococcus pneumoniae / cytology*
  • Streptococcus pneumoniae / metabolism*
  • Tritium

Substances

  • Bacterial Proteins
  • Carbon Isotopes
  • Cell Cycle Proteins
  • FtsX protein, bacteria
  • Nitrogen Isotopes
  • Tritium