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Structural comparison between the major capsid proteins of OmRV-LZ and ScV-L-A.

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posted on 2021-03-17, 17:40 authored by Qianqian Shao, Xudong Jia, Yuanzhu Gao, Zhe Liu, Huan Zhang, Qiqi Tan, Xin Zhang, Huiqiong Zhou, Yinyin Li, De Wu, Qinfen Zhang

(A) Superposition of MCP-A in OmRV-LZ (blue) and ScV-L-A (pink). (B) Zoomed-in view of the region framed by the yellow dotted box in panel B, showing five pairs of α-helices (labelled α1–5) with conserved folds between OmRV-LZ and ScV-L-A. Other mismatched structures are set to translucent for clarity. (C, D) Zoomed-in view of the region framed by the green dotted box in panel B. (C) Atomic model of the cap-snatching reaction centre in ScV-L-A. The sidechain of the active site His154 (coloured pink) and nearby key residues Tyr150, His151, Asp152, Tyr452, Tyr538 and Asp540 that may be involved in the cap-snatching reaction (coloured grey) are displayed. (D) Atomic model of the region in OmRV-LZ MCP-A corresponding to the cap-snatching reaction centre of ScV-L-A MCP-A. All sidechains in this region are displayed.

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