Fig. 4: C-terminal region of LACV-L FL. | Nature Communications

Fig. 4: C-terminal region of LACV-L FL.

From: Pre-initiation and elongation structures of full-length La Crosse virus polymerase reveal functionally important conformational changes

Fig. 4

a The structure of LACV-L C-terminal region is shown as non-transparent, the rest of the polymerase is shown as transparent, except the residues interacting with the ZBD β-hairpin strut. The domains are colored as in Fig. 1. Position of the last α-helix 91 that interacts with α-helices 88/89 is indicated and a close-up view of hydrophobic amino acids interaction is shown. Close-up view on the coordination of the presumed zinc ion from the ZBD. Conserved residues implicated in ion coordination are shown and labeled. The ZBD β-hairpin strut that protrudes towards the core is surrounded by a dotted rectangle corresponding to panel b view. b Close-up view of the ZBD β-hairpin strut. Residues from the core lobe β-hairpin (705–724) and the palm domain that interact with the ZBD β-hairpin are indicated. The active site is surrounded by a dotted line.

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