Extensive Mutagenesis Experiments Corroborate a Structural Model for the DNA Deaminase Domain of APOBEC3G

Overview

Journal FEBS Lett

Specialty Biochemistry

Date 2007 Sep 18

PMID 17869248

Citations 40

Authors

Kuan-Ming Chen

Natalia Martemyanova

Yongjian Lu

Keisuke Shindo

Hiroshi Matsuo

Reuben S Harris

Affiliations

Soon will be listed here.

Abstract

APOBEC3G is a single-strand DNA cytosine deaminase capable of blocking retrovirus and retrotransposon replication. APOBEC3G has two conserved zinc-coordinating motifs but only one is required for catalysis. Here, deletion analyses revealed that the minimal catalytic domain consists of residues 198-384. Size exclusion assays indicated that this protein is monomeric. Many (31/69) alanine substitution derivatives of APOBEC3G198-384 retained significant to full levels of activity. These data corroborated an APOBEC2-based structural model for the catalytic domain of APOBEC3G indicating that most non-essential residues are solvent accessible and most essential residues cluster within the protein core.

Citing Articles

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Structural and functional assessment of APOBEC3G macromolecular complexes.

Polevoda B, McDougall W, Bennett R, Salter J, Smith H Methods. 2016; 107:10-22.

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