3J4U

A new topology of the HK97-like fold revealed in Bordetella bacteriophage: non-covalent chainmail secured by jellyrolls

3J4U の概要

• エントリーDOI: 10.2210/pdb3j4u/pdb
• EMDBエントリー: 5764 5765 5766
• 分子名称: major capsid protein, cementing protein (2 entities in total)
• 機能のキーワード: protein topology, cryoem, virus
• 由来する生物種: Bordetella phage BPP-1; 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 356470.48

構造登録者

Zhang, X.,Guo, H.,Jin, L.,Czornyj, E.,Hodes, A.,Hui, W.H.,Nieh, A.W.,Miller, J.F.,Zhou, Z.H. (登録日: 2013-10-09, 公開日: 2013-12-25, 最終更新日: 2024-02-21)

主引用文献

Zhang, X.,Guo, H.,Jin, L.,Czornyj, E.,Hodes, A.,Hui, W.H.,Nieh, A.W.,Miller, J.F.,Zhou, Z.H.
A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5 A resolution.
Elife, 2:e01299-e01299, 2013

PubMed Abstract: Bacteriophage BPP-1 infects and kills Bordetella species that cause whooping cough. Its diversity-generating retroelement (DGR) provides a naturally occurring phage-display system, but engineering efforts are hampered without atomic structures. Here, we report a cryo electron microscopy structure of the BPP-1 head at 3.5 Å resolution. Our atomic model shows two of the three protein folds representing major viral lineages: jellyroll for its cement protein (CP) and HK97-like ('Johnson') for its major capsid protein (MCP). Strikingly, the fold topology of MCP is permuted non-circularly from the Johnson fold topology previously seen in viral and cellular proteins. We illustrate that the new topology is likely the only feasible alternative of the old topology. β-sheet augmentation and electrostatic interactions contribute to the formation of non-covalent chainmail in BPP-1, unlike covalent inter-protein linkages of the HK97 chainmail. Despite these complex interactions, the termini of both CP and MCP are ideally positioned for DGR-based phage-display engineering. DOI: http://dx.doi.org/10.7554/eLife.01299.001.

PubMed: 24347545
DOI: 10.7554/eLife.01299

実験手法

ELECTRON MICROSCOPY (3.5 Å)