PDBsum entry 3kml

Viral protein

PDB id: 3kml

Contents

Protein chains

(+ 11 more) 141 a.a. *

* Residue conservation analysis

PDB id:

3kml

Name:

Viral protein

Title:

Circular permutant of the tobacco mosaic virus

Structure:

Coat protein. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q. Engineered: yes. Mutation: yes

Source:

Tobacco mosaic virus. Tmv. Organism_taxid: 12243. Strain: u1. Gene: cp. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

3.01Å R-factor: 0.240 R-free: 0.253

Authors:

K.E.Duderstadt,M.T.Dedeo,M.B.Francis,J.M.Berger

Key ref:

M.T.Dedeo et al. (2010). Nanoscale protein assemblies from a circular permutant of the tobacco mosaic virus. Nano Lett, 10, 181-186. PubMed id: 19924865

Date:

10-Nov-09 Release date: 16-Feb-10

Protein chains

P69687  (CAPSD_TMV) -  Capsid protein from Tobacco mosaic virus (strain vulgare)

Seq: 159 a.a.

Struc: 141 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Nano Lett 10:181-186 (2010)

PubMed id: 19924865

Nanoscale protein assemblies from a circular permutant of the tobacco mosaic virus.

M.T.Dedeo, K.E.Duderstadt, J.M.Berger, M.B.Francis.

ABSTRACT

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.