Crystal structure of DNA cytidine deaminase ABOBEC3G catalytic deamination domain suggests a binding mode of full-length enzyme to single-stranded DNA

Abstract

Background: The mechanism for DNA cytidine deaminase APOBEC3G (A3G) interacting with single-stranded DNA (ssDNA) is not well characterized. Results: The crystal structure of a head-to-tail dimer of the A3G catalytic deamination domain (A3G-CD2) was obtained. Conclusion: The dimer structure of A3G-CD2 suggests a binding mode of full-length A3G to ssDNA. Significance: The dimer structure of A3G-CD2 may represent a structural model of full-length A3G.