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Crystal Structure of the SF3 Helicase from Adeno-Associated Virus Type 2

Authors
Journal
Structure
0969-2126
Publisher
Elsevier
Publication Date
Volume
11
Issue
8
Identifiers
DOI: 10.1016/s0969-2126(03)00152-7
Disciplines
  • Biology

Abstract

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.

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