Cryo-EM structure of a molluscan hemocyanin suggests its allosteric mechanism.

Cryo-EM structure of a molluscan hemocyanin suggests its allosteric mechanism.
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DOI:
10.1016/j.str.2013.02.018
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发表时间:
2013-04-02
期刊:
影响因子:
5.7
通讯作者:
Chiu, Wah
Chiu, Wah
中科院分区:
生物学2区
文献类型:
--
作者:
Zhang, Qinfen;Dai, Xinghong;Cong, Yao;Zhang, Junjie;Chen, Dong-Hua;Dougherty, Matthew T.;Wang, Jiangyong;Ludtke, Steven J.;Schmid, Michael F.;Chiu, Wah

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Hemocyanins are responsible for transporting O2 in the arthropod and molluscan hemolymph. Haliotis diversicolor molluscan hemocyanin isoform 1 (HdH1) is an 8 MDa oligomer. Each subunit is made up of eight functional units (FUs). Each FU contains two Cu ions, which can reversibly bind an oxygen molecule. Here we report a ~4.5 Å cryo-EM structure of HdH1. The structure clearly shows 10 asymmetric units arranged with D5 symmetry. Each asymmetric unit contains two structurally distinct but chemically identical subunits. The map is sufficiently resolved to trace the entire subunit Cα backbone, and to visualize densities corresponding to some large sidechains, Cu ion pairs, and interaction networks of adjacent subunits. A FU topology path intertwining between the two subunits of the asymmetric unit is unambiguously determined. Our observations suggest a structural mechanism for the stability of the entire hemocyanin didecamer and 20 “communication clusters” across asymmetric units responsible for its allosteric property upon oxygen binding.
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