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PDBsum entry 3kml
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Viral protein
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PDB id
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3kml
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References listed in PDB file
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Key reference
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Title
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Nanoscale protein assemblies from a circular permutant of the tobacco mosaic virus.
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Authors
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M.T.Dedeo,
K.E.Duderstadt,
J.M.Berger,
M.B.Francis.
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Ref.
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Nano Lett, 2010,
10,
181-186.
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PubMed id
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Abstract
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The protein coat of the tobacco mosaic virus (TMV) has been explored extensively
for the construction of nanoscale architectures. In previous work, we have
reported efficient TMV-based light harvesting systems bearing chromophores in a
hollow channel of the assembled protein. We have also reported an N-terminal
transamination/oximation method that could be used to attach electrodes and
catalytic groups to the exterior surface of the rods. To complement these
techniques, we report herein a new circular permutant of the TMV capsid protein
that repositions the N- and C-termini to the center of the assemblies. This
protein can be produced in very high yield through E. coli expression and
self-assembles into light harvesting rods that are much like those assembled
from the wild-type protein. However, the disks formed from the permutant
structure are stable over a significantly wider pH range, greatly improving the
practicality of this assembled form for materials applications. The new position
of the N-terminus allows functional groups to be installed in the inner pore of
the disks, affording geometries reminiscent of natural photosynthetic systems.
The permutant also shows the ability to coassemble with regular monomers,
allowing the future generation of multicomponent rod structures that are
modified on the exterior and interior surfaces, as well as in the internal RNA
channel.
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