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Bluetongue virus VP4 is an RNA-capping assembly line


Eukaryotic organisms cap the 5′ ends of their messenger RNAs by a series of four chemical reactions. Some viruses achieve this using a single molecule; the crystal structure of such an enzyme from bluetongue virus reveals an elongated modular architecture that provides a scaffold for an assemblage of active sites, two contributed by a domain of novel structure.

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Figure 1: Overall structure of VP4.
Figure 2: The structure of the methyltransferase domains and ligands.
Figure 3: Structure of the N- and C-terminal domains.

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We thank L. Lyne, W. Lu and the staff of BM14 and ID14 beamlines at the European Synchrotron Radiation Facility for technical support. This work was supported by the Medical Research Council, UK, EC SPINE grant QLG2-CT-2002-00988 (D.I.S.), and by the Royal Society, UK (J.M.G.).

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Correspondence to David I Stuart or Polly Roy.

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Supplementary information

Supplementary Fig. 1

Overview of the structure. (PDF 9119 kb)

Supplementary Fig. 2

Electron density map and Cα trace. (PDF 4865 kb)

Supplementary Fig. 3

Stereo view of crystal dimer. (PDF 2492 kb)

Supplementary Fig. 4

The 2′ OMT domain. (PDF 7201 kb)

Supplementary Fig. 5

The N7MT domain. (PDF 4734 kb)

Supplementary Fig. 6

The N- and C-terminal domains. (PDF 4052 kb)

Supplementary Table 1

Data collection, phasing and refinement statistics for VP4 structure. (PDF 58 kb)

Supplementary Methods (PDF 89 kb)

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Sutton, G., Grimes, J., Stuart, D. et al. Bluetongue virus VP4 is an RNA-capping assembly line. Nat Struct Mol Biol 14, 449–451 (2007).

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