1FR5

PHAGE FR CAPSIDS WITH A FOUR RESIDUE DELETION IN THE COAT PROTEIN FG LOOP

1FR5 の概要

• エントリーDOI: 10.2210/pdb1fr5/pdb
• 分子名称: BACTERIOPHAGE FR CAPSID (1 entity in total)
• 機能のキーワード: viral coat protein, capsid, icosahedral virus, virus
• 由来する生物種: Enterobacteria phage fr
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 40001.95

構造登録者

Axblom, C.,Tars, K.,Fridborg, K.,Bundule, M.,Orna, L.,Liljas, L. (登録日: 1998-07-22, 公開日: 1999-01-13, 最終更新日: 2024-05-22)

主引用文献

Axblom, C.,Tars, K.,Fridborg, K.,Orna, L.,Bundule, M.,Liljas, L.
Structure of phage fr capsids with a deletion in the FG loop: implications for viral assembly.
Virology, 249:80-88, 1998

PubMed Abstract: The loop between beta-strands F and G in the coat protein of small RNA bacteriophages forms the interactions at the fivefold and threefold (quasi-sixfold) icosahedral axes. In many cases, mutations in this region renders the coat protein unable to form capsids. This FG loop has therefore been suggested to be of major importance for the virus assembly process by guiding the assembly and helping to define the correct curvature of the virus shell. We have determined the crystal structure of a phage fr capsid where the coat protein has a four-residue deletion in the FG loop. This mutant retains the ability to form virus capsids of normal size but has a significantly lower temperature stability than the wild type. The structure reveals that the mutated loops are flexible and too short to interact with each other. This seems incompatible with a role of the FG loop in the regulation of capsid size.

PubMed: 9740779
DOI: 10.1006/viro.1998.9279

実験手法

X-RAY DIFFRACTION (3.5 Å)