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	Alternative conformations and motions adopted by 30S ribosomal subunits visualized by cryo-electron microscopy.
ジャーナル・号・ページ	RNA, Vol. 26, Issue 12, Page 2017-2030, Year 2020
掲載日	2020年9月28日
著者	Dushyant Jahagirdar / Vikash Jha / Kaustuv Basu / Josue Gomez-Blanco / Javier Vargas / Joaquin Ortega /
PubMed 要旨	It is only after recent advances in cryo-electron microscopy that it is now possible to describe at high-resolution structures of large macromolecules that do not crystalize. Purified 30S subunits ...It is only after recent advances in cryo-electron microscopy that it is now possible to describe at high-resolution structures of large macromolecules that do not crystalize. Purified 30S subunits interconvert between an "active" and "inactive" conformation. The active conformation was described by crystallography in the early 2000s, but the structure of the inactive form at high resolution remains unsolved. Here we used cryo-electron microscopy to obtain the structure of the inactive conformation of the 30S subunit to 3.6 Å resolution and study its motions. In the inactive conformation, an alternative base-pairing of three nucleotides causes the region of helix 44, forming the decoding center to adopt an unlatched conformation and the 3' end of the 16S rRNA positions similarly to the mRNA during translation. Incubation of inactive 30S subunits at 42°C reverts these structural changes. The air-water interface to which ribosome subunits are exposed during sample preparation also peel off some ribosomal proteins. Extended exposures to low magnesium concentrations make the ribosomal particles more susceptible to the air-water interface causing the unfolding of large rRNA structural domains. Overall, this study provides new insights about the conformational space explored by the 30S ribosomal subunit when the ribosomal particles are free in solution.
リンク	RNA / PubMed:32989043 / PubMed Central
手法	EM (単粒子)
解像度	3.2 - 4.5 Å
構造データ	21558 6w6k EMDB-21558, PDB-6w6k: 30S-Activated-high-Mg2+ 手法: EM (単粒子) / 解像度: 3.6 Å 21569 6w77 EMDB-21569, PDB-6w77: 30S-Inactivated-high-Mg2+ Class A 手法: EM (単粒子) / 解像度: 3.6 Å EMDB-21570: 30S-Inactive-high-Mg2+ Class B 手法: EM (単粒子) / 解像度: 4.5 Å 21571 6w7m EMDB-21571, PDB-6w7m: 30S-Inactive-high-Mg2+ + carbon layer 手法: EM (単粒子) / 解像度: 3.8 Å 21572 6w7n EMDB-21572, PDB-6w7n: 30S-Inactive-low-Mg2+ Class A 手法: EM (単粒子) / 解像度: 3.4 Å 21573 6w7w EMDB-21573, PDB-6w7w: 30S-Inactive-low-Mg2+ Class B 手法: EM (単粒子) / 解像度: 3.9 Å EMDB-22690: 30S-Inactive-low-Mg2+ Carbon 手法: EM (単粒子) / 解像度: 3.2 Å
化合物	ChemComp-MG: Unknown entry / マグネシウムジカチオン
由来	Escherichia coli K-12 (大腸菌) escherichia coli (strain k12) (大腸菌)
キーワード	RIBOSOME (リボソーム) / 30S subunit / conformations / inactive / activated