7UU3

Crystal structure of APOBEC3G complex with 3'overhangs RNA-Complex

Summary for 7UU3

• Entry DOI: 10.2210/pdb7uu3/pdb
• Descriptor: DNA dC->dU-editing enzyme APOBEC-3G, RNA (5'-R(*CP*CP*CP*AP*CP*GP*GP*GP*AP*AP*U)-3'), RNA (5'-R(*CP*CP*CP*GP*UP*GP*GP*GP*AP*AP*U)-3'), ... (4 entities in total)
• Functional Keywords: deaminase, apobec, hydrolase, hydrolase-rna complex, hydrolase/rna
• Biological source: Macaca mulatta (Rhesus monkey); More
• Total number of polymer chains: 4
• Total formula weight: 99414.90

Authors

Yang, H.,Li, S.,Chen, X.S. (deposition date: 2022-04-28, release date: 2023-01-11, Last modification date: 2023-10-25)

Primary citation

Yang, H.,Kim, K.,Li, S.,Pacheco, J.,Chen, X.S.
Structural basis of sequence-specific RNA recognition by the antiviral factor APOBEC3G.
Nat Commun, 13:7498-7498, 2022

PubMed Abstract: An essential step in restricting HIV infectivity by the antiviral factor APOBEC3G is its incorporation into progeny virions via binding to HIV RNA. However, the mechanism of APOBEC3G capturing viral RNA is unknown. Here, we report crystal structures of a primate APOBEC3G bound to different types of RNAs, revealing that APOBEC3G specifically recognizes unpaired 5'-AA-3' dinucleotides, and to a lesser extent, 5'-GA-3' dinucleotides. APOBEC3G binds to the common 3'A in the AA/GA motifs using an aromatic/hydrophobic pocket in the non-catalytic domain. It binds to the 5'A or 5'G in the AA/GA motifs using an aromatic/hydrophobic groove conformed between the non-catalytic and catalytic domains. APOBEC3G RNA binding property is distinct from that of the HIV nucleocapsid protein recognizing unpaired guanosines. Our findings suggest that the sequence-specific RNA recognition is critical for APOBEC3G virion packaging and restricting HIV infectivity.

PubMed: 36470880
DOI: 10.1038/s41467-022-35201-9

Experimental method

X-RAY DIFFRACTION (3.099 Å)