8HMH
The closed state of RGLG2-VWA
8HMH の概要
エントリーDOI | 10.2210/pdb8hmh/pdb |
分子名称 | E3 ubiquitin-protein ligase RGLG2, MAGNESIUM ION (3 entities in total) |
機能のキーワード | closed state, calcium ions, plant protein, transferase, structural protein |
由来する生物種 | Arabidopsis thaliana (thale cress) |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 68947.77 |
構造登録者 | |
主引用文献 | Zhang, M.,Zhang, J.,Liang, Y.,Tian, S.,Xie, S.,Zhou, T.,Wang, Q. The regulation of RGLG2-VWA by Ca 2+ ions. Biochim Biophys Acta Proteins Proteom, 1872:140966-140966, 2024 Cited by PubMed 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 Ca ions are allosteric regulators of RGLG2-VWA, which adopts open state when NCBS1(Novel Calcium ions Binding Site 1) binds Ca ions and switches to closed state after Ca 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 Ca ions in conformational change of VWA domain. In addition, we found that RGLG2, corresponding to low affinity, can bind pseudo-ligand, which has never been observed in other VWA domains. PubMed: 37734561DOI: 10.1016/j.bbapap.2023.140966 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.56 Å) |
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