Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA

Maiti, Atanu; Myint, Wazo; Kanai, Tapan; Delviks-Frankenberry, Krista; Rodriguez, Christina Sierra; Pathak, Vinay K.; Schiffer, Celia A.; Matsuo, Hiroshi

doi:10.1038/s41467-018-04872-8

Crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA

Journal Article · Mon Jun 25 00:00:00 EDT 2018 · Nature Communications

DOI:https://doi.org/10.1038/s41467-018-04872-8· OSTI ID:1461696

^[1]; ^[1]; ^[1]; ^[2]; Rodriguez, Christina Sierra ^[1]; Pathak, Vinay K. ^[2]; ^[3]; ^[1]

Frederick National Lab. for Cancer Research, MD (United States)
National Cancer Inst. at Frederick, MD (United States)
Univ. of Massachusetts, Worcester, MA (United States)

The human APOBEC3G protein is a cytidine deaminase that generates cytidine to deoxy-uridine mutations in single-stranded DNA (ssDNA), and capable of restricting replication of HIV-1 by generating mutations in viral genome. The mechanism by which APOBEC3G specifically deaminates 5'-CC motifs has remained elusive since structural studies have been hampered due to apparently weak ssDNA binding of the catalytic domain of APOBEC3G. We overcame the problem by generating a highly active variant with higher ssDNA affinity. Here, we present the crystal structure of this variant complexed with a ssDNA substrate at 1.86 Å resolution. This structure reveals atomic-level interactions by which APOBEC3G recognizes a functionally-relevant 5'-TCCCA sequence. This complex also reveals a key role of W211 in substrate recognition, implicating a similar recognition in activation-induced cytidine deaminase (AID) with a conserved tryptophan.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: National Inst. of Health; National Cancer Inst.

OSTI ID:: 1461696

Journal Information:: Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 9; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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