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	Structural basis for dynamic regulation of the human 26S proteasome.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 113, Issue 46, Page 12991-12996, Year 2016
掲載日	2016年11月15日
著者	Shuobing Chen / Jiayi Wu / Ying Lu / Yong-Bei Ma / Byung-Hoon Lee / Zhou Yu / Qi Ouyang / Daniel J Finley / Marc W Kirschner / Youdong Mao /
PubMed 要旨	The proteasome is the major engine of protein degradation in all eukaryotic cells. At the heart of this machine is a heterohexameric ring of AAA (ATPases associated with diverse cellular activities) ...The proteasome is the major engine of protein degradation in all eukaryotic cells. At the heart of this machine is a heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitylated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. Using cryoelectron microscopy, we determined a near-atomic-resolution structure of the 2.5-MDa human proteasome in its ground state, as well as subnanometer-resolution structures of the holoenzyme in three alternative conformational states. The substrate-unfolding AAA-ATPase channel is narrowed by 10 inward-facing pore loops arranged into two helices that run in parallel with each other, one hydrophobic in character and the other highly charged. The gate of the core particle was unexpectedly found closed in the ground state and open in only one of the alternative states. Coordinated, stepwise conformational changes of the regulatory particle couple ATP hydrolysis to substrate translocation and regulate gating of the core particle, leading to processive degradation.
リンク	Proc Natl Acad Sci U S A / PubMed:27791164 / PubMed Central
手法	EM (単粒子)
解像度	3.8 - 8.0 Å
構造データ	8332 5t0c EMDB-8332, PDB-5t0c: Structural basis for dynamic regulation of the human 26S proteasome 手法: EM (単粒子) / 解像度: 3.8 Å 8333 5t0c EMDB-8333, PDB-5t0c: Structural basis for dynamic regulation of the human 26S proteasome 手法: EM (単粒子) / 解像度: 3.8 Å 8334 5t0g EMDB-8334, PDB-5t0g: Structural basis for dynamic regulation of the human 26S proteasome 手法: EM (単粒子) / 解像度: 4.4 Å 8335 5t0h EMDB-8335, PDB-5t0h: Structural basis for dynamic regulation of the human 26S proteasome 手法: EM (単粒子) / 解像度: 6.8 Å 8336 5t0i EMDB-8336, PDB-5t0i: Structural basis for dynamic regulation of the human 26S proteasome 手法: EM (単粒子) / 解像度: 8.0 Å 8337 5t0j EMDB-8337, PDB-5t0j: Structural basis for dynamic regulation of the human 26S proteasome 手法: EM (単粒子) / 解像度: 8.0 Å
化合物	ChemComp-ZN: Unknown entry ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM
由来	homo sapiens (ヒト)
キーワード	HYDROLASE / ubiquitin-proteasome system / AAA-ATPase