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1H, 15N, and 13C chemical shift backbone resonance NMR assignment of the accumulation-associated protein (Aap) lectin domain from Staphylococcus epidermidis
Biomolecular NMR Assignments ( IF 0.9 ) Pub Date : 2023-04-06 , DOI: 10.1007/s12104-023-10126-6
Rahul Yadav 1, 2 , Tanveer Shaikh 1 , Suhas Tikole 1 , Andrew B Herr 3 , Nicholas C Fitzkee 1
Affiliation  

Staphylococcus epidermidis is the leading causative agent for hospital-acquired infections, especially device-related infections, due to its ability to form biofilms. The accumulation-associated protein (Aap) of S. epidermidis is primarily responsible for biofilm formation and consists of two domains, A and B. It was found that the A domain is responsible for the attachment to the abiotic/biotic surface, whereas the B domain is responsible for the accumulation of bacteria during biofilm formation. One of the parts of the A domain is the Aap lectin, which is a carbohydrate-binding domain having 222 amino acids in its structure. Here we report the near complete backbone chemical shift assignments for the lectin domain, as well as its predicted secondary structure. This data will provide a platform for future NMR studies to explore the role of lectin in biofilm formation.



中文翻译:

表皮葡萄球菌积累相关蛋白 (Aap) 凝集素结构域的 1H、15N 和 13C 化学位移骨架共振 NMR 分配

表皮葡萄球菌是医院获得性感染的主要病原体,尤其是设备相关感染,因为它能够形成生物膜。表皮葡萄球菌的积累相关蛋白 (Aap)主要负责生物膜的形成,由 A 和 B 两个结构域组成。发现 A 结构域负责附着在非生物/生物表面,而 B 结构域负责生物膜形成过程中细菌的积累。A 域的一部分是 Aap 凝集素,它是一个碳水化合物结合域,其结构中有 222 个氨基酸。在这里,我们报告了凝集素结构域的近乎完整的骨架化学位移分配,以及其预测的二级结构。该数据将为未来的 NMR 研究提供一个平台,以探索凝集素在生物膜形成中的作用。

更新日期:2023-04-06
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