5K82

Crystal Structure of a Primate APOBEC3G N-Terminal Domain

Summary for 5K82

• Entry DOI: 10.2210/pdb5k82/pdb
• Related: 5K81 5K83
• Descriptor: Apolipoprotein B mRNA editing enzyme, catalytic peptide-like 3G,Apolipoprotein B mRNA editing enzyme, catalytic peptide-like 3G, ZINC ION (2 entities in total)
• Functional Keywords: apobec3g, vif, hiv, apobec, hydrolase
• Biological source: Macaca mulatta (Rhesus macaque); More
• Total number of polymer chains: 4
• Total formula weight: 92632.77

Authors

Xiao, X.,Li, S.-X.,Yang, H.,Chen, X.S. (deposition date: 2016-05-27, release date: 2016-08-10, Last modification date: 2023-09-27)

Primary citation

Xiao, X.,Li, S.X.,Yang, H.,Chen, X.S.
Crystal structures of APOBEC3G N-domain alone and its complex with DNA.
Nat Commun, 7:12193-12193, 2016

PubMed 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.

PubMed: 27480941
DOI: 10.1038/ncomms12193

Experimental method

X-RAY DIFFRACTION (2.913 Å)