Complete non-proline backbone resonance assignments of the S. aureus neutrophil serine protease inhibitor, EapH1

IF 0.8 4区生物学 Q4 BIOPHYSICS

Biomolecular NMR Assignments Pub Date : 2023-05-10 DOI:10.1007/s12104-023-10131-9

Nitin Mishra, Indrani Pal, Alvaro I. Herrera, Abhinav Dubey, Haribabu Arthanari, Brian V. Geisbrecht, Om Prakash

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引用次数: 1

Abstract

The S. aureus extracellular adherence protein (Eap) and its homologs, EapH1 and EapH2, serve roles in evasion of the human innate immune system. EapH1 binds with high-affinity and inhibits the neutrophil azurophilic granule proteases neutrophil elastase, cathepsin-G and proteinase-3. Previous structural studies using X-ray crystallography have shown that EapH1 binds to neutrophil elastase and cathepsin-G using a globally similar binding mode. However, whether the same holds true in solution is unknown and whether the inhibitor experiences dynamic changes following binding remains uncertain. To facilitate solution-phase structural and biochemical studies of EapH1 and its complexes with neutrophil granule proteases, we have characterized EapH1 by multidimensional NMR spectroscopy. Here we report a total of 100% of the non-proline backbone resonance assignments of EapH1 with BMRB accession number 50,304.

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金黄色葡萄球菌中性粒细胞丝氨酸蛋白酶抑制剂EapH1的完全非脯氨酸骨干共振分配

金黄色葡萄球菌细胞外粘附蛋白(Eap)及其同源物EapH1和EapH2在逃避人类先天免疫系统中起作用。EapH1以高亲和力结合并抑制中性粒细胞颗粒蛋白酶、中性粒细胞弹性蛋白酶、组织蛋白酶- g和蛋白酶-3。先前使用x射线晶体学进行的结构研究表明，EapH1与中性粒细胞弹性蛋白酶和组织蛋白酶- g的结合模式是全局相似的。然而，在溶液中是否同样成立是未知的，并且抑制剂在结合后是否经历动态变化仍然不确定。为了便于对EapH1及其与中性粒细胞颗粒蛋白酶复合物的溶液相结构和生化研究，我们利用多维核磁共振光谱对EapH1进行了表征。在这里，我们报告了BMRB编码号为50304的EapH1的非脯氨酸主干共振分配的100%。

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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.