The regulation of RGLG2-VWA by Ca2+ ions

IF 2.5 4区生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY Biochimica et biophysica acta. Proteins and proteomics Pub Date : 2023-09-19 DOI:10.1016/j.bbapap.2023.140966

MeiLing Zhang , JiaXiang Zhang , Yan Liang, ShiCheng Tian, ShuYang Xie, Tong Zhou, Qin Wang

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Abstract

RGLG2, an E3 ubiquitin ligase in Arabidopsis thaliana, affects hormone signaling and participates in drought regulation. Here, we determined two crystal structures of RGLG2 VWA domain, representing two conformations, open and closed, respectively. The two structures reveal that Ca²⁺ ions are allosteric regulators of RGLG2-VWA, which adopts open state when NCBS1(Novel Calcium ions Binding Site 1) binds Ca²⁺ ions and switches to closed state after Ca²⁺ ions are removed. This mechanism of allosteric regulation is identical to RGLG1-VWA, but distinct from integrin α and β VWA domains. Therefore, our data provide a backdrop for understanding the role of the Ca²⁺ ions in conformational change of VWA domain. In addition, we found that RGLG2^closed, corresponding to low affinity, can bind pseudo-ligand, which has never been observed in other VWA domains.

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Ca2+离子对RGLG2-VWA的调控

RGLG2是拟南芥E3泛素连接酶，影响激素信号并参与干旱调控。在这里，我们确定了RGLG2 VWA域的两种晶体结构，分别代表两种构象，开放和封闭。这两种结构表明Ca2+离子是RGLG2-VWA的变构调节剂，当NCBS1(Novel Calcium ions Binding Site 1)与Ca2+离子结合时，RGLG2-VWA处于开放状态，Ca2+离子去除后，RGLG2-VWA进入封闭状态。这种变构调节机制与RGLG1-VWA相同，但与整合素α和β VWA结构域不同。因此，我们的数据为理解Ca2+离子在VWA结构域构象变化中的作用提供了一个背景。此外，我们发现RGLG2closed，对应于低亲和力，可以结合伪配体，这在其他VWA结构域中从未观察到。

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来源期刊

Biochimica et biophysica acta. Proteins and proteomics 生物-生化与分子生物学

CiteScore

8.00

自引率

0.00%

发文量

审稿时长

33 days

期刊介绍： BBA Proteins and Proteomics covers protein structure conformation and dynamics; protein folding; protein-ligand interactions; enzyme mechanisms, models and kinetics; protein physical properties and spectroscopy; and proteomics and bioinformatics analyses of protein structure, protein function, or protein regulation.