8V8B

Structure of 80alpha portal protein expressed in E. coli

8V8B の概要

• エントリーDOI: 10.2210/pdb8v8b/pdb
• EMDBエントリー: 43033
• 分子名称: Portal protein (1 entity in total)
• 機能のキーワード: complex, phage, sapi, portal, structural protein
• 由来する生物種: Staphylococcus phage 80alpha
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59551.82

構造登録者

Kizziah, J.L.,Mukherjee, A.,Dokland, T. (登録日: 2023-12-05, 公開日: 2024-01-10, 最終更新日: 2024-01-17)

主引用文献

Mukherjee, A.,Kizziah, J.L.,Hawkins, N.C.,Nasef, M.O.,Parker, L.K.,Dokland, T.
Structure of the Portal Complex from Staphylococcus aureus Pathogenicity Island 1 Transducing Particles In Situ and In Isolation.
J.Mol.Biol., 436:168415-168415, 2023

PubMed Abstract: Staphylococcus aureus is an important human pathogen, and the prevalence of antibiotic resistance is a major public health concern. The evolution of pathogenicity and resistance in S. aureus often involves acquisition of mobile genetic elements (MGEs). Bacteriophages play an especially important role, since transduction represents the main mechanism for horizontal gene transfer. S. aureus pathogenicity islands (SaPIs), including SaPI1, are MGEs that carry genes encoding virulence factors, and are mobilized at high frequency through interactions with specific "helper" bacteriophages, such as 80α, leading to packaging of the SaPI genomes into virions made from structural proteins supplied by the helper. Among these structural proteins is the portal protein, which forms a ring-like portal at a fivefold vertex of the capsid, through which the DNA is packaged during virion assembly and ejected upon infection of the host. We have used high-resolution cryo-electron microscopy to determine structures of the S. aureus bacteriophage 80α portal itself, produced by overexpression, and in situ in the empty and full SaPI1 virions, and show how the portal interacts with the capsid. These structures provide a basis for understanding portal and capsid assembly and the conformational changes that occur upon DNA packaging and ejection.

PubMed: 38135177
DOI: 10.1016/j.jmb.2023.168415

実験手法

ELECTRON MICROSCOPY (2.4 Å)