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 of the Borrelia Bacteriophage φBB1 Procapsid.
ジャーナル・号・ページ	J Mol Biol, Vol. 435, Issue 24, Page 168323, Year 2023
掲載日	2023年12月15日
著者	Jānis Rūmnieks / Tibor Füzik / Kaspars Tārs /
PubMed 要旨	Bacteriophages of Borrelia burgdorferi are a biologically important but under-investigated feature of the Lyme disease-causing spirochete. No virulent borrelial viruses have been identified, but all ...Bacteriophages of Borrelia burgdorferi are a biologically important but under-investigated feature of the Lyme disease-causing spirochete. No virulent borrelial viruses have been identified, but all B. burgdorferi isolates carry a prophage φBB1 as resident circular plasmids. Like its host, the φBB1 phage is quite distinctive and shares little sequence similarity with other known bacteriophages. We expressed φBB1 head morphogenesis proteins in Escherichia coli which resulted in assembly of homogeneous prolate procapsid structures and used cryo-electron microscopy to determine the three-dimensional structure of these particles. The φBB1 procapsids consist of 415 copies of the major capsid protein and an equal combined number of three homologous capsid decoration proteins that form trimeric knobs on the outside of the particle. One of the end vertices of the particle is occupied by a portal assembled from twelve copies of the portal protein. The φBB1 scaffolding protein is entirely α-helical and has an elongated shape with a small globular domain in the middle. Within the tubular section of the procapsid, the internal scaffold is built of stacked rings, each composed of 32 scaffolding protein molecules, which run in opposite directions from both caps with a heterogeneous part in the middle. Inside the portal-containing cap, the scaffold is organized asymmetrically with ten scaffolding protein molecules bound to the portal. The φBB1 procapsid structure provides better insight into the vast structural diversity of bacteriophages and presents clues of how elongated bacteriophage particles might be assembled.
リンク	J Mol Biol / PubMed:37866476
手法	EM (単粒子)
解像度	2.34 - 10.62 Å
構造データ	17669 8pho EMDB-17669, PDB-8pho: Portal from the Borrelia bacteriophage BB1 procapsid 手法: EM (単粒子) / 解像度: 2.34 Å 17670 8php EMDB-17670, PDB-8php: Portal from the Borrelia bacteriophage BB1 procapsid with bound scaffold protein 手法: EM (単粒子) / 解像度: 2.56 Å 17671 8phq EMDB-17671, PDB-8phq: Top cap of the Borrelia bacteriophage BB1 procapsid, fivefold-symmetrized outer shell 手法: EM (単粒子) / 解像度: 2.69 Å 17672 8phr EMDB-17672, PDB-8phr: Middle part of the Borrelia bacteriophage BB1 procapsid, tenfold-symmetrized outer shell 手法: EM (単粒子) / 解像度: 2.65 Å 17673 8phs EMDB-17673, PDB-8phs: Bottom cap of the Borrelia bacteriophage BB1 procapsid, fivefold-symmetrized outer shell 手法: EM (単粒子) / 解像度: 2.82 Å 17674 8pht EMDB-17674, PDB-8pht: Scaffold rings inside the Borrelia bacteriophage BB1 procapsid 手法: EM (単粒子) / 解像度: 6.37 Å 17675 8phu EMDB-17675, PDB-8phu: Asymmetric structure of the portal-containing cap of the Borrelia bacteriophage BB1 procapsid 手法: EM (単粒子) / 解像度: 7.41 Å 17739 8pkh EMDB-17739, PDB-8pkh: Borrelia bacteriophage BB1 procapsid, fivefold-symmetrized outer shell 手法: EM (単粒子) / 解像度: 3.35 Å 18518 8qo0 EMDB-18518, PDB-8qo0: Asymmetric structure of the Borrelia bacteriophage BB1 procapsid, 3D class 2 手法: EM (単粒子) / 解像度: 10.62 Å 18519 8qo1 EMDB-18519, PDB-8qo1: Asymmetric structure of the Borrelia bacteriophage BB1 procapsid, 3D class 3 手法: EM (単粒子) / 解像度: 9.76 Å
化合物	ChemComp-HOH: WATER
由来	borreliella burgdorferi b31 (バクテリア)
キーワード	VIRAL PROTEIN / Bacteriophage / portal / DNA packaging / scaffold / capsid / procapsid