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	Initial location of the RNA-dependent RNA polymerase in the bacteriophage Phi6 procapsid determined by cryo-electron microscopy.
ジャーナル・号・ページ	J Biol Chem, Vol. 283, Issue 18, Page 12227-12231, Year 2008
掲載日	2008年5月2日
著者	Anindito Sen / J Bernard Heymann / Naiqian Cheng / Jian Qiao / Leonard Mindich / Alasdair C Steven /
PubMed 要旨	The RNA-dependent RNA polymerases (RdRPs) of Cystoviridae bacteriophages, like those of eukaryotic viruses of the Reoviridae, function inside the inner capsid shell in both replication and ...The RNA-dependent RNA polymerases (RdRPs) of Cystoviridae bacteriophages, like those of eukaryotic viruses of the Reoviridae, function inside the inner capsid shell in both replication and transcription. In bacteriophage Phi6, this inner shell is first assembled as an icosahedral procapsid with recessed 5-fold vertices that subsequently undergoes major structural changes during maturation. The tripartite genome is packaged as single-stranded RNA molecules via channels on the 5-fold vertices, and transcripts probably exit the mature capsid by the same route. The RdRP (protein P2) is assembled within the procapsid, and it was thought that it should be located on the 5-fold axes near the RNA entry and exit channels. To determine the initial location of the RdRP inside the procapsid of bacteriophage Phi6, we performed cryo-electron microscopy of wild type and mutant procapsids and complemented these data with biochemical determinations of copy numbers. We observe ring-like densities on the 3-fold axes that are strong in a mutant that has approximately 10 copies of P2 per particle; faint in wild type, reflecting the lower copy number of approximately 3; and completely absent in a P2-null mutant. The dimensions and shapes of these densities match those of the known crystal structure of the P2 monomer. We propose that, during maturation, the P2 molecules rotate to occupy positions closer to adjacent 5-fold vertices where they conduct replication and transcription.
リンク	J Biol Chem / PubMed:18287088 / PubMed Central
手法	EM (単粒子)
解像度	11.0 - 19.0 Å
構造データ	EMDB-1500: Initial location of the RNA-dependent RNA polymerase in the bacteriophage phi6 procapsid determined by cryo-electron microscopy 手法: EM (単粒子) / 解像度: 14.0 Å EMDB-1501: Initial location of the RNA-dependent RNA polymerase in the bacteriophage phi6 procapsid determined by cryo-electron microscopy 手法: EM (単粒子) / 解像度: 19.0 Å EMDB-1502: Initial location of the RNA-dependent RNA polymerase in the bacteriophage phi6 procapsid determined by cryo-electron microscopy 手法: EM (単粒子) / 解像度: 11.0 Å EMDB-1503: Initial location of the RNA-dependent RNA polymerase in the bacteriophage phi6 procapsid determined by cryo-electron microscopy 手法: EM (単粒子) / 解像度: 16.0 Å