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	Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex.
ジャーナル・号・ページ	Sci Adv, Vol. 7, Issue 46, Page eabj9537, Year 2021
掲載日	2021年11月12日
著者	Shanshan Li / Kan-Yen Hsieh / Chiao-I Kuo / Shih-Chieh Su / Kai-Fa Huang / Kaiming Zhang / Chung-I Chang /
PubMed 要旨	The Lon protease is the prototype of a family of proteolytic machines with adenosine triphosphatase modules built into a substrate degradation chamber. Lon is known to degrade protein substrates in a ...The Lon protease is the prototype of a family of proteolytic machines with adenosine triphosphatase modules built into a substrate degradation chamber. Lon is known to degrade protein substrates in a processive fashion, cutting a protein chain processively into small peptides before commencing cleavages of another protein chain. Here, we present structural and biochemical evidence demonstrating that processive substrate degradation occurs at each of the six proteolytic active sites of Lon, which forms a deep groove that partially encloses the substrate polypeptide chain by accommodating only the unprimed residues and permits processive cleavage in the C-to-N direction. We identify a universally conserved acidic residue at the exit side of the binding groove indispensable for the proteolytic activity. This noncatalytic residue likely promotes processive proteolysis by carboxyl-carboxylate interactions with cleaved intermediates. Together, these results uncover a previously unrecognized mechanism for processive substrate degradation by the Lon protease.
リンク	Sci Adv / PubMed:34757797 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	2.1 - 3.28 Å
構造データ	31589 7fid EMDB-31589, PDB-7fid: Processive cleavage of substrate at individual proteolytic active sites of the Lon proteasecomplex (conformation 1) 手法: EM (単粒子) / 解像度: 2.44 Å 31590 7fie EMDB-31590, PDB-7fie: Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex (conformation 2) 手法: EM (単粒子) / 解像度: 2.36 Å 31607 7fiz EMDB-31607, PDB-7fiz: Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex (conformation 3) 手法: EM (単粒子) / 解像度: 3.28 Å PDB-7eux: Crystal structure of the Lon-like protease MtaLonC with D581A mutation in complex with substrate polypeptide 手法: X-RAY DIFFRACTION / 解像度: 2.25 Å PDB-7euy: Crystal structure of the Lon-like protease MtaLonC with D582A mutation in complex with substrate polypeptide 手法: X-RAY DIFFRACTION / 解像度: 2.2 Å PDB-7ev4: Crystal structure of the Lon-like protease MtaLonC with S582A mutation in complex with F-b20-Q 手法: X-RAY DIFFRACTION / 解像度: 2.12 Å PDB-7ev6: Crystal structure of the Lon-like protease MtaLonC with D581A mutation in complex with F-b20-Q 手法: X-RAY DIFFRACTION / 解像度: 2.1 Å
化合物	ChemComp-PO4: PHOSPHATE ION / ホスファ-ト ChemComp-HOH: WATER 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-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM
由来	meiothermus taiwanensis wr-220 (バクテリア) meiothermus taiwanensis (バクテリア) escherichia coli (大腸菌)
キーワード	HYDROLASE / protease / TTC1975 peptidase / Lon-like protease / AAA / complex / proteolysis