Journal
STRUCTURE
Volume 11, Issue 8, Pages 1025-1035Publisher
CELL PRESS
DOI: 10.1016/S0969-2126(03)00152-7
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Funding
- NIAID NIH HHS [R01 AI41706] Funding Source: Medline
- NIGMS NIH HHS [R01 GM62234] Funding Source: Medline
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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.
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