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	CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin.
ジャーナル・号・ページ	Nat Commun, Vol. 12, Issue 1, Page 4754, Year 2021
掲載日	2021年8月6日
著者	Yanyan Zhao / Michael F Schmid / Judith Frydman / Wah Chiu /
PubMed 要旨	Chaperonins are homo- or hetero-oligomeric complexes that use ATP binding and hydrolysis to facilitate protein folding. ATP hydrolysis exhibits both positive and negative cooperativity. The mechanism ...Chaperonins are homo- or hetero-oligomeric complexes that use ATP binding and hydrolysis to facilitate protein folding. ATP hydrolysis exhibits both positive and negative cooperativity. The mechanism by which chaperonins coordinate ATP utilization in their multiple subunits remains unclear. Here we use cryoEM to study ATP binding in the homo-oligomeric archaeal chaperonin from Methanococcus maripaludis (MmCpn), consisting of two stacked rings composed of eight identical subunits each. Using a series of image classification steps, we obtained different structural snapshots of individual chaperonins undergoing the nucleotide binding process. We identified nucleotide-bound and free states of individual subunits in each chaperonin, allowing us to determine the ATP occupancy state of each MmCpn particle. We observe distinctive tertiary and quaternary structures reflecting variations in nucleotide occupancy and subunit conformations in each chaperonin complex. Detailed analysis of the nucleotide distribution in each MmCpn complex indicates that individual ATP binding events occur in a statistically random manner for MmCpn, both within and across the rings. Our findings illustrate the power of cryoEM to characterize a biochemical property of multi-subunit ligand binding cooperativity at the individual particle level.
リンク	Nat Commun / PubMed:34362932 / PubMed Central
手法	EM (単粒子)
解像度	3.9 - 6.4 Å
構造データ	24324 7r9e EMDB-24324, PDB-7r9e: Methanococcus maripaludis chaperonin, open conformation 1 手法: EM (単粒子) / 解像度: 4.0 Å 24325 7r9h EMDB-24325, PDB-7r9h: Methanococcus maripaludis chaperonin, open conformation 2 手法: EM (単粒子) / 解像度: 6.3 Å 24326 7r9i EMDB-24326, PDB-7r9i: Methanococcus maripaludis chaperonin, open conformation 2 手法: EM (単粒子) / 解像度: 6.4 Å 24327 7r9j EMDB-24327, PDB-7r9j: Methanococcus maripaludis chaperonin, open conformation 4 手法: EM (単粒子) / 解像度: 6.3 Å 24328 7r9k EMDB-24328, PDB-7r9k: Methanococcus maripaludis chaperonin, closed conformation 4 手法: EM (単粒子) / 解像度: 4.1 Å 24329 7r9m EMDB-24329, PDB-7r9m: Methanococcus maripaludis chaperonin, closed conformation 2 手法: EM (単粒子) / 解像度: 4.0 Å 24330 7r9o EMDB-24330, PDB-7r9o: Methanococcus maripaludis chaperonin, closed conformation 1 手法: EM (単粒子) / 解像度: 4.0 Å 24331 7r9u EMDB-24331, PDB-7r9u: Methanococcus maripaludis chaperonin, closed conformation 3 手法: EM (単粒子) / 解像度: 4.4 Å 24363 7rak EMDB-24363, PDB-7rak: Methanococcus maripaludis chaperonin complex in open conformation 手法: EM (単粒子) / 解像度: 3.9 Å
化合物	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子*YM
由来	methanococcus maripaludis (古細菌)
キーワード	CHAPERONE / Open conformation / Closed conformation / Complex / chaperonin.