4NSD

Crystal Structure of CBARA1 in the Ca2+ Binding Form

4NSD の概要

• エントリーDOI: 10.2210/pdb4nsd/pdb
• 関連するPDBエントリー: 4NSC
• 分子名称: Calcium uptake protein 1, mitochondrial, CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: ef-hand, calcium binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion inner membrane; Peripheral membrane protein: Q9BPX6
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81546.14

構造登録者

Wang, L.,Yang, X.,Li, S.,Shen, Y. (登録日: 2013-11-28, 公開日: 2014-02-26, 最終更新日: 2024-02-28)

主引用文献

Wang, L.,Yang, X.,Li, S.,Wang, Z.,Liu, Y.,Feng, J.,Zhu, Y.,Shen, Y.
Structural and mechanistic insights into MICU1 regulation of mitochondrial calcium uptake.
Embo J., 33:594-604, 2014

PubMed Abstract: Mitochondrial calcium uptake is a critical event in various cellular activities. Two recently identified proteins, the mitochondrial Ca(2+) uniporter (MCU), which is the pore-forming subunit of a Ca(2+) channel, and mitochondrial calcium uptake 1 (MICU1), which is the regulator of MCU, are essential in this event. However, the molecular mechanism by which MICU1 regulates MCU remains elusive. In this study, we report the crystal structures of Ca(2+)-free and Ca(2+)-bound human MICU1. Our studies reveal that Ca(2+)-free MICU1 forms a hexamer that binds and inhibits MCU. Upon Ca(2+) binding, MICU1 undergoes large conformational changes, resulting in the formation of multiple oligomers to activate MCU. Furthermore, we demonstrate that the affinity of MICU1 for Ca(2+) is approximately 15-20 μM. Collectively, our results provide valuable details to decipher the molecular mechanism of MICU1 regulation of mitochondrial calcium uptake.

PubMed: 24514027
DOI: 10.1002/embj.201386523

実験手法

X-RAY DIFFRACTION (2.7 Å)