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. Author manuscript; available in PMC: 2016 Oct 29.
Published in final edited form as: Nature. 2015 Oct 26;527(7579):531–534. doi: 10.1038/nature15767

Figure 4. Interactions between TEC and capsid shell proteins (CSPs).

Figure 4

a-b, Conformational changes of modules A (yellow loops/helices as wires/cylinders) and B (magenta loops/helices as wires/cylinders) in quiescent (a) and transcribing (b) states. Module A interacts with the capsid shell, and the loop-Bα5 fragment of module B blocks the active site (inset) in the quiescent state (a) but retracts to expose the active site in the transcribing (b) state (see Extended Data Figure 7). c-d, The RdRP-bound dsRNA (ribbon) in the quiescent state (c) is detached from RdRP in the transcribing state (d). e-f, Interactions of CSPs (ribbons) with RdRP (purple and yellow) and VP4 (cyan). Residues of RdRP and VP4 within 4Å distance to the capsid shell are marked in red. An icosahedral 5-fold axis is indicated by a green line in (e) and a green pentagon in (f). Insets in (f) indicate two CSP N-terminal helices (white density with ribbon-and-stick models): one (upper) interacts only with RdRP while the other (lower) with both RdRP and VP4.