MeiLing Zhang , JiaXiang Zhang , Yan Liang, ShiCheng Tian, ShuYang Xie, Tong Zhou, Qin Wang
{"title":"The regulation of RGLG2-VWA by Ca2+ ions","authors":"MeiLing Zhang , JiaXiang Zhang , Yan Liang, ShiCheng Tian, ShuYang Xie, Tong Zhou, Qin Wang","doi":"10.1016/j.bbapap.2023.140966","DOIUrl":null,"url":null,"abstract":"<div><p><span>RGLG2, an E3 ubiquitin ligase in </span><span><em>Arabidopsis thaliana</em></span>, 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 Ca<sup>2+</sup><span> ions are allosteric regulators of RGLG2-VWA, which adopts open state when NCBS1(Novel Calcium ions Binding Site 1) binds Ca</span><sup>2+</sup> ions and switches to closed state after Ca<sup>2+</sup><span><span> ions are removed. This mechanism of allosteric regulation is identical to RGLG1-VWA, but distinct from </span>integrin α and β VWA domains. Therefore, our data provide a backdrop for understanding the role of the Ca</span><sup>2+</sup><span> ions in conformational change of VWA domain. In addition, we found that RGLG2</span><sup>closed</sup>, corresponding to low affinity, can bind pseudo-ligand, which has never been observed in other VWA domains.</p></div>","PeriodicalId":2,"journal":{"name":"ACS Applied Bio Materials","volume":null,"pages":null},"PeriodicalIF":4.6000,"publicationDate":"2023-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"ACS Applied Bio Materials","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1570963923000808","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"MATERIALS SCIENCE, BIOMATERIALS","Score":null,"Total":0}
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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 RGLG2closed, corresponding to low affinity, can bind pseudo-ligand, which has never been observed in other VWA domains.
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