Crystal structure of the SF3 helicase from adeno-associated virus type 2

J A James, C R Escalante, M Yoon-Robarts, T A Edwards, R M Linden, A K Aggarwal

Research output: Contribution to journalArticlepeer-review

106 Citations (Scopus)

Abstract

We report here the crystal structure of an SF3 DNA helicase, Rep40, from adeno-associated virus 2 (AAV2). We show that AAV2 Rep40 is structurally more similar to the AAA(+) class of cellular proteins than to DNA helicases from other superfamilies. The structure delineates the expected Walker A and B motifs, but also reveals an unexpected "arginine finger" that directly implies the requirement of Rep40 oligomerization for ATP hydrolysis and helicase activity. Further, the Rep40 AAA(+) domain is novel in that it is unimodular as opposed to bimodular. Altogether, the structural connection to AAA(+) proteins defines the general architecture of SF3 DNA helicases, a family that includes simian virus 40 (SV40) T antigen, as well as provides a conceptual framework for understanding the role of Rep proteins during AAV DNA replication, packaging, and site-specific integration
Original languageEnglish
Pages (from-to)1025 - 1035
Number of pages11
JournalStructure
Volume11
Issue number8
DOIs
Publication statusPublished - 1 Aug 2003

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