Crystal structures of APOBEC3G N-domain alone and its complex with DNA

Xiao Xiao, Shu-Xing Li, Hanjing Yang and Xiaojiang S. Chen ()
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Xiao Xiao: Genetic, Molecular and Cellular Biology Program, Keck School of Medicine, University of Southern California
Shu-Xing Li: Molecular and Computational Biology Program, University of Southern California
Hanjing Yang: Molecular and Computational Biology Program, University of Southern California
Xiaojiang S. Chen: Genetic, Molecular and Cellular Biology Program, Keck School of Medicine, University of Southern California

Nature Communications, 2016, vol. 7, issue 1, 1-11

Abstract: Abstract APOBEC3G (A3G) is a potent restriction factor of HIV-1. The N-terminal domain of A3G (A3G-CD1) is responsible for oligomerization and nucleic acid binding, both of which are essential for anti-HIV activity. As a countermeasure, HIV-1 viral infectivity factor (Vif) binds A3G-CD1 to mediate A3G degradation. The structural basis for the functions of A3G-CD1 remains elusive. Here, we report the crystal structures of a primate A3G-CD1 (rA3G-CD1) alone and in complex with single-stranded DNA (ssDNA). rA3G-CD1 shares a conserved core structure with the previously determined catalytic APOBECs, but displays unique features for surface charge, dimerization and nucleic acid binding. Its co-crystal structure with ssDNA reveals how the conformations of loops and residues surrounding the Zn-coordinated centre (Zn-centre) change upon DNA binding. The dimerization interface of rA3G-CD1 is important for oligomerization, nucleic acid binding and Vif-mediated degradation. These findings elucidate the molecular basis of antiviral mechanism and HIV-Vif targeting of A3G.

Date: 2016
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DOI: 10.1038/ncomms12193

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