Department of Chemistry, Indiana University, Bloomington, Indiana, USA.
Graduate Program in Biochemistry, Indiana University, Bloomington, Indiana, USA.
Biomol NMR Assign. 2020 Oct;14(2):233-238. doi: 10.1007/s12104-020-09952-9. Epub 2020 Jun 3.
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, C and N 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.
肺炎链球菌是一种革兰氏阳性的人类病原体,在全球范围内导致数百万人感染,并且抗生素耐药性的发生率不断增加。铁的获取对于其生存和毒力至关重要,特别是在宿主施加的营养免疫下。肺炎链球菌表达几种 ATP 结合盒(ABC)转运蛋白来促进在缺铁条件下的获取,包括 PitABCD、PiaABCD 和 PiuBCDA。PiuBCDA 的底物特异性尚未完全确定。在此,我们报告了apo 形式和与 Ga(III)以及儿茶酚类铁载体类似物 4-LICAM 复合物中可溶性、细胞外结构域的 31 kDa 可溶性底物结合蛋白 PiuA 的 H、C 和 N 共振归属。这些研究为进一步研究与其他蛋白质、金属和小分子的相互作用提供了有价值的信息。