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	Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis.
ジャーナル・号・ページ	Nat Struct Mol Biol, Vol. 27, Issue 5, Page 406-416, Year 2020
掲載日	2020年4月20日
著者	Kyle E Lopez / Alexandrea N Rizo / Eric Tse / JiaBei Lin / Nathaniel W Scull / Aye C Thwin / Aaron L Lucius / James Shorter / Daniel R Southworth /
PubMed 要旨	The ClpAP complex is a conserved bacterial protease that unfolds and degrades proteins targeted for destruction. The ClpA double-ring hexamer powers substrate unfolding and translocation into the ...The ClpAP complex is a conserved bacterial protease that unfolds and degrades proteins targeted for destruction. The ClpA double-ring hexamer powers substrate unfolding and translocation into the ClpP proteolytic chamber. Here, we determined high-resolution structures of wild-type Escherichia coli ClpAP undergoing active substrate unfolding and proteolysis. A spiral of pore loop-substrate contacts spans both ClpA AAA+ domains. Protomers at the spiral seam undergo nucleotide-specific rearrangements, supporting substrate translocation. IGL loops extend flexibly to bind the planar, heptameric ClpP surface with the empty, symmetry-mismatched IGL pocket maintained at the seam. Three different structures identify a binding-pocket switch by the IGL loop of the lowest positioned protomer, involving release and re-engagement with the clockwise pocket. This switch is coupled to a ClpA rotation and a network of conformational changes across the seam, suggesting that ClpA can rotate around the ClpP apical surface during processive steps of translocation and proteolysis.
リンク	Nat Struct Mol Biol / PubMed:32313240 / PubMed Central
手法	EM (単粒子)
解像度	2.7 - 3.4 Å
構造データ	20845 6uqe EMDB-20845, PDB-6uqe: ClpA/ClpP Disengaged State bound to RepA-GFP 手法: EM (単粒子) / 解像度: 3.0 Å 20851 6uqo EMDB-20851, PDB-6uqo: ClpA/ClpP Engaged State bound to RepA-GFP 手法: EM (単粒子) / 解像度: 3.1 Å 21519 6w1z EMDB-21519, PDB-6w1z: ClpAP Engaged1 State bound to RepA-GFP 手法: EM (単粒子) / 解像度: 2.7 Å 21520 6w20 EMDB-21520, PDB-6w20: ClpAP Disengaged State bound to RepA-GFP 手法: EM (単粒子) / 解像度: 3.0 Å 21521 6w21 EMDB-21521, PDB-6w21: ClpAP Engaged2 State bound to RepA-GFP 手法: EM (単粒子) / 解像度: 3.3 Å 21522 6w22 EMDB-21522, PDB-6w22: ClpA Engaged1 State bound to RepA-GFP (ClpA Focused Refinement) 手法: EM (単粒子) / 解像度: 3.0 Å 21523 6w23 EMDB-21523, PDB-6w23: ClpA Disengaged State bound to RepA-GFP (Focused Classification) 手法: EM (単粒子) / 解像度: 3.1 Å 21524 6w24 EMDB-21524, PDB-6w24: ClpA Engaged2 State bound to RepA-GFP (Focused Classification) 手法: EM (単粒子) / 解像度: 3.4 Å
化合物	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM ChemComp-AGS: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-γ-S / ATP-gamma-S, エネルギー貯蔵分子類似体YM ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子*YM
由来	escherichia coli k-12 (大腸菌) unidentified (未定義) escherichia coli (strain k12) (大腸菌) escherichia coli (大腸菌) synthetic construct (人工物)
キーワード	CHAPERONE / AAA+ / Protease / Hsp100 / ATPase