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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.