Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 14, Issue 2, Pages 233-238Publisher
SPRINGER
DOI: 10.1007/s12104-020-09952-9
Keywords
Iron acquisition; ABC transporter; Pathogen; Catechol; Siderophore; Streptococcus pneumoniae
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Funding
- US National Institutes of Health [R35 GM118157]
- UK Engineering and Physical Sciences Research Council [EP/L024829/1]
- EPSRC [EP/L024829/1] Funding Source: UKRI
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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 H-1, C-13 and N-15 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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