6IBC

Thermophage P23-45 procapsid

6IBC の概要

• エントリーDOI: 10.2210/pdb6ibc/pdb
• 関連するPDBエントリー: 6I9E
• EMDBエントリー: 4433 4447
• 分子名称: Major head protein (1 entity in total)
• 機能のキーワード: bacteriophage, thermophage, caudovirales, siphoviridae, capsid, procapsid, auxiliary, hk97, virus
• 由来する生物種: Thermus virus P23-45
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 326765.28

構造登録者

Bayfield, O.W.,Klimuk, E.,Winkler, D.C.,Hesketh, E.L.,Chechik, M.,Cheng, N.,Dykeman, E.C.,Minakhin, L.,Ranson, N.A.,Severinov, K.,Steven, A.C.,Antson, A.A. (登録日: 2018-11-29, 公開日: 2019-02-13, 最終更新日: 2024-07-10)

主引用文献

Bayfield, O.W.,Klimuk, E.,Winkler, D.C.,Hesketh, E.L.,Chechik, M.,Cheng, N.,Dykeman, E.C.,Minakhin, L.,Ranson, N.A.,Severinov, K.,Steven, A.C.,Antson, A.A.
Cryo-EM structure and in vitro DNA packaging of a thermophilic virus with supersized T=7 capsids.
Proc. Natl. Acad. Sci. U.S.A., 116:3556-3561, 2019

PubMed Abstract: Double-stranded DNA viruses, including bacteriophages and herpesviruses, package their genomes into preformed capsids, using ATP-driven motors. Seeking to advance structural and mechanistic understanding, we established in vitro packaging for a thermostable bacteriophage, P23-45 of Both the unexpanded procapsid and the expanded mature capsid can package DNA in the presence of packaging ATPase over the 20 °C to 70 °C temperature range, with optimum activity at 50 °C to 65 °C. Cryo-EM reconstructions for the mature and immature capsids at 3.7-Å and 4.4-Å resolution, respectively, reveal conformational changes during capsid expansion. Capsomer interactions in the expanded capsid are reinforced by formation of intersubunit β-sheets with N-terminal segments of auxiliary protein trimers. Unexpectedly, the capsid has T=7 quasi-symmetry, despite the P23-45 genome being twice as large as those of known T=7 phages, in which the DNA is compacted to near-crystalline density. Our data explain this anomaly, showing how the canonical HK97 fold has adapted to double the volume of the capsid, while maintaining its structural integrity. Reconstructions of the procapsid and the expanded capsid defined the structure of the single vertex containing the portal protein. Together with a 1.95-Å resolution crystal structure of the portal protein and DNA packaging assays, these reconstructions indicate that capsid expansion affects the conformation of the portal protein, while still allowing DNA to be packaged. These observations suggest a mechanism by which structural events inside the capsid can be communicated to the outside.

PubMed: 30737287
DOI: 10.1073/pnas.1813204116

実験手法

ELECTRON MICROSCOPY (4.39 Å)