EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Asymmetric apical domain states of mitochondrial Hsp60 coordinate substrate engagement and chaperonin assembly.
ジャーナル・号・ページ	bioRxiv, Year 2023
掲載日	2023年5月15日
著者	Julian R Braxton / Hao Shao / Eric Tse / Jason E Gestwicki / Daniel R Southworth /
PubMed 要旨	The mitochondrial chaperonin, mtHsp60, promotes the folding of newly imported and transiently misfolded proteins in the mitochondrial matrix, assisted by its co-chaperone mtHsp10. Despite its ...The mitochondrial chaperonin, mtHsp60, promotes the folding of newly imported and transiently misfolded proteins in the mitochondrial matrix, assisted by its co-chaperone mtHsp10. Despite its essential role in mitochondrial proteostasis, structural insights into how this chaperonin binds to clients and progresses through its ATP-dependent reaction cycle are not clear. Here, we determined cryo-electron microscopy (cryo-EM) structures of a hyperstable disease-associated mtHsp60 mutant, V72I, at three stages in this cycle. Unexpectedly, client density is identified in all states, revealing interactions with mtHsp60's apical domains and C-termini that coordinate client positioning in the folding chamber. We further identify a striking asymmetric arrangement of the apical domains in the ATP state, in which an alternating up/down configuration positions interaction surfaces for simultaneous recruitment of mtHsp10 and client retention. Client is then fully encapsulated in mtHsp60/mtHsp10, revealing prominent contacts at two discrete sites that potentially support maturation. These results identify a new role for the apical domains in coordinating client capture and progression through the cycle, and suggest a conserved mechanism of group I chaperonin function.
リンク	bioRxiv / PubMed:37293102 / PubMed Central
手法	EM (単粒子)
解像度	2.5 - 3.8 Å
構造データ	29813 8g7j EMDB-29813, PDB-8g7j: mtHsp60 V72I apo 手法: EM (単粒子) / 解像度: 3.4 Å 29814 8g7k EMDB-29814, PDB-8g7k: mtHsp60 V72I apo focus 手法: EM (単粒子) / 解像度: 3.8 Å 29815 8g7l EMDB-29815, PDB-8g7l: ATP-bound mtHsp60 V72I 手法: EM (単粒子) / 解像度: 2.5 Å 29816 8g7m EMDB-29816, PDB-8g7m: ATP-bound mtHsp60 V72I focus 手法: EM (単粒子) / 解像度: 3.2 Å 29817 8g7n EMDB-29817, PDB-8g7n: ATP- and mtHsp10-bound mtHsp60 V72I 手法: EM (単粒子) / 解像度: 2.7 Å 29818 8g7o EMDB-29818, PDB-8g7o: ATP- and mtHsp10-bound mtHsp60 V72I focus 手法: EM (単粒子) / 解像度: 3.4 Å
化合物	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-K*: Unknown entry / カリウムカチオン
由来	homo sapiens (ヒト)
キーワード	CHAPERONE / chaperonin / ATPase / foldase