8HMH
The closed state of RGLG2-VWA
Summary for 8HMH
| Entry DOI | 10.2210/pdb8hmh/pdb |
| Descriptor | E3 ubiquitin-protein ligase RGLG2, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | closed state, calcium ions, plant protein, transferase, structural protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 68947.77 |
| Authors | Wang, Q. (deposition date: 2022-12-03, release date: 2023-12-27, Last modification date: 2024-11-13) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.56 Å) |
Structure validation
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