1H, 15N, and 13C chemical shift backbone resonance NMR assignment of the accumulation-associated protein (Aap) lectin domain from Staphylococcus epidermidis

IF 0.8 4区生物学 Q4 BIOPHYSICS

Biomolecular NMR Assignments Pub Date : 2023-04-06 DOI:10.1007/s12104-023-10126-6

Rahul Yadav, Tanveer Shaikh, Suhas Tikole, Andrew B. Herr, Nicholas C. Fitzkee

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Abstract

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.

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表皮葡萄球菌积累相关蛋白(Aap)凝集素结构域的1H, 15N和13C化学位移骨干核磁共振分配

表皮葡萄球菌是医院获得性感染的主要病原体，特别是与器械相关的感染，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。研究发现，A结构域负责附着于非生物/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结构域的一个部分是Aap凝集素，这是一个碳水化合物结合结构域，其结构中有222个氨基酸。在这里，我们报告了凝集素结构域近乎完整的主链化学位移分配，以及其预测的二级结构。这些数据将为未来的核磁共振研究探索凝集素在生物膜形成中的作用提供一个平台。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Biomolecular NMR Assignments 生物-光谱学

CiteScore

1.70

自引率

11.10%

发文量

审稿时长

6-12 weeks

期刊介绍： Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.