7PV2

GA1 bacteriophage portal protein

7PV2 の概要

• エントリーDOI: 10.2210/pdb7pv2/pdb
• EMDBエントリー: 13664
• 分子名称: Head-tail connector (Portal protein) (1 entity in total)
• 機能のキーワード: bacteriophage, portal protein, cryoem, viral protein
• 由来する生物種: Bacillus phage GA-1
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 423693.61

構造登録者

Javed, A.,Villanueva, H.,Orlova, E.V.,Savva, R. (登録日: 2021-10-01, 公開日: 2022-10-12, 最終更新日: 2023-10-25)

主引用文献

Javed, A.,Villanueva, H.,Shataer, S.,Vasciaveo, S.,Savva, R.,Orlova, E.V.
Cryo-EM Structures of Two Bacteriophage Portal Proteins Provide Insights for Antimicrobial Phage Engineering.
Viruses, 13:-, 2021

PubMed Abstract: Widespread antibiotic resistance has returned attention to bacteriophages as a means of managing bacterial pathogenesis. Synthetic biology approaches to engineer phages have demonstrated genomic editing to broaden natural host ranges, or to optimise microbicidal action. Gram positive pathogens cause serious pastoral animal and human infections that are especially lethal in newborns. Such pathogens are targeted by the obligate lytic phages of the and families. These phages have relatively small ~20 kb linear protein-capped genomes and their compact organisation, relatively few structural elements, and broad host range, are appealing from a phage-engineering standpoint. In this study, we focus on portal proteins, which are core elements for the assembly of such tailed phages. The structures of dodecameric portal complexes from phage GA1, which targets , and phage phiCPV4 that infects , were determined at resolutions of 3.3 Å and 2.9 Å, respectively. Both are found to closely resemble the related phi29 portal protein fold. However, the portal protein of phiCPV4 exhibits interesting differences in the clip domain. These structures provide new insights on structural diversity in portal proteins and will be essential for considerations in phage structural engineering.

PubMed: 34960800
DOI: 10.3390/v13122532

実験手法

ELECTRON MICROSCOPY (3.2 Å)