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	Structure and conformational cycle of a bacteriophage-encoded chaperonin.
ジャーナル・号・ページ	PLoS One, Vol. 15, Issue 4, Page e0230090, Year 2020
掲載日	2020年4月27日
著者	Andreas Bracher / Simanta S Paul / Huping Wang / Nadine Wischnewski / F Ulrich Hartl / Manajit Hayer-Hartl /
PubMed 要旨	Chaperonins are ubiquitous molecular chaperones found in all domains of life. They form ring-shaped complexes that assist in the folding of substrate proteins in an ATP-dependent reaction cycle. Key ...Chaperonins are ubiquitous molecular chaperones found in all domains of life. They form ring-shaped complexes that assist in the folding of substrate proteins in an ATP-dependent reaction cycle. Key to the folding cycle is the transient encapsulation of substrate proteins by the chaperonin. Here we present a structural and functional characterization of the chaperonin gp146 (ɸEL) from the phage EL of Pseudomonas aeruginosa. ɸEL, an evolutionarily distant homolog of bacterial GroEL, is active in ATP hydrolysis and prevents the aggregation of denatured protein in a nucleotide-dependent manner. However, ɸEL failed to refold the encapsulation-dependent model substrate rhodanese and did not interact with E. coli GroES, the lid-shaped co-chaperone of GroEL. ɸEL forms tetradecameric double-ring complexes, which dissociate into single rings in the presence of ATP. Crystal structures of ɸEL (at 3.54 and 4.03 Å) in presence of ATP•BeFx revealed two distinct single-ring conformational states, both with open access to the ring cavity. One state showed uniform ATP-bound subunit conformations (symmetric state), whereas the second combined distinct ATP- and ADP-bound subunit conformations (asymmetric state). Cryo-electron microscopy of apo-ɸEL revealed a double-ring structure composed of rings in the asymmetric state (3.45 Å resolution). We propose that the phage chaperonin undergoes nucleotide-dependent conformational switching between double- and single rings and functions in aggregation prevention without substrate protein encapsulation. Thus, ɸEL may represent an evolutionarily more ancient chaperonin prior to acquisition of the encapsulation mechanism.
リンク	PLoS One / PubMed:32339190 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	3.45 - 5.91 Å
構造データ	10528 6tmv EMDB-10528, PDB-6tmv: Structure of the chaperonin gp146 from the bacteriophage EL (Pseudomonas aeruginosa) in the apo state 手法: EM (単粒子) / 解像度: 3.45 Å 10529 6tmw EMDB-10529, PDB-6tmw: Structure of the chaperonin gp146 from the bacteriophage EL (Pseudomonas aeruginosa) in complex with ADP 手法: EM (単粒子) / 解像度: 5.91 Å 10530 6tmx EMDB-10530, PDB-6tmx: Structure of the chaperonin gp146 from the bacteriophage EL (Pseudomonas aeruginosa) in complex with ATPgammaS 手法: EM (単粒子) / 解像度: 5.8 Å PDB-6tmt: Crystal structure of the chaperonin gp146 from the bacteriophage EL 2 (Pseudomonas aeruginosa) in presence of ATP-BeFx, crystal form I 手法: X-RAY DIFFRACTION / 解像度: 4.03 Å PDB-6tmu: Crystal structure of the chaperonin gp146 from the bacteriophage EL 2 (Pseudomonas aeruginosa) in presence of ATP-BeFx, crystal form II 手法: X-RAY DIFFRACTION / 解像度: 3.54 Å
化合物	ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM / アデノシン三リン酸 ChemComp-K: Unknown entry / カリウムカチオン ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM / アデノシン二リン酸 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
由来	pseudomonas phage el (ファージ)
キーワード	CHAPERONE (シャペロン) / molecular chaperone (シャペロン) / ATPase (ATPアーゼ) / chaperonin