1H, 13C, 15N backbone resonance assignments of the apo and holo forms of the ABC transporter solute binding protein PiuA from Streptococcus pneumoniae


Streptococcus pneumoniae is a Gram-positive human pathogen that causes millions of infections worldwide with an increasing occurrence of antibiotic resistance. Iron acquisition is essential for its survival and virulence, especially under host-imposed nutritional immunity. S. pneumoniae expresses several ATP-binding cassette (ABC) transporters to facilitate acquisition under iron limitation, including PitABCD, PiaABCD, and PiuBCDA. The substrate specificity of PiuBCDA is not fully established. Herein, we report the backbone 1H, 13C and 15N resonance assignments of the 31 kDa soluble, extracellular domain of the substrate binding protein PiuA in the apo form and in complex with Ga(III) and the catechol siderophore-mimic 4-LICAM. These studies provide valuable information for further functional studies of interactions with other proteins, metals, and small molecules.

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This research was supported by US National Institutes of Health grant R35 GM118157 to D.P.G. and UK Engineering and Physical Sciences Research Council grant EP/L024829/1 to A.K.D.K. We thank Dr. Hongwei Wu for technical assistance.

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Correspondence to David P. Giedroc.

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Edmonds, K.A., Zhang, Y., Raines, D.J. et al. 1H, 13C, 15N backbone resonance assignments of the apo and holo forms of the ABC transporter solute binding protein PiuA from Streptococcus pneumoniae. Biomol NMR Assign 14, 233–238 (2020). https://doi.org/10.1007/s12104-020-09952-9

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  • Iron acquisition
  • ABC transporter
  • Pathogen
  • Catechol
  • Siderophore
  • Streptococcus pneumoniae