Isolating a trimer intermediate in the self-assembly of E2 protein cage.

Abstract:

:Understanding the self-assembly mechanism of caged proteins provides clues to develop their potential applications in nanotechnology, such as a nanoscale drug delivery system. The E2 protein from Bacillus stearothermophilus , with a virus-like caged structure, has drawn much attention for its potential application as a nanocapsule. To investigate its self-assembly process from subunits to a spherical protein cage, we truncate the C-terminus of the E2 subunit. The redesigned protein subunit shows dynamic transition between monomer and trimer, but not the integrate 60-mer. The results indicate the role of the trimer as the intermediate and building block during the self-assembly of the E2 protein cage. In combination with the molecular dynamics simulations results, we conclude that the C-terminus modulates the self-assembly of the E2 protein cage from trimer to 60-mer. This investigation elucidates the role of the intersubunit interactions in engineering other functionalities in other caged structure proteins.

journal_name

Biomacromolecules

journal_title

Biomacromolecules

authors

Peng T,Lee H,Lim S

doi

10.1021/bm201587q

subject

Has Abstract

pub_date

2012-03-12 00:00:00

pages

699-705

issue

3

eissn

1525-7797

issn

1526-4602

journal_volume

13

pub_type

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