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

期刊

BIOMOLECULAR NMR ASSIGNMENTS
卷 14, 期 2, 页码 233-238

出版社

SPRINGER
DOI: 10.1007/s12104-020-09952-9

关键词

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

资金

  1. US National Institutes of Health [R35 GM118157]
  2. UK Engineering and Physical Sciences Research Council [EP/L024829/1]
  3. 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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