TY - JOUR
T1 - Crystal structure of the SF3 helicase from adeno-associated virus type 2
AU - James, J. Anson
AU - Escalante, Carlos R.
AU - Yoon-Robarts, Miran
AU - Edwards, Thomas A.
AU - Linden, R. Michael
AU - Aggarwal, Aneel K.
N1 - Funding Information:
We thank the staff at beamlines 14BM (APS) and X6A (NSLS) for facilitating X-ray data collection. A.K.A. is supported by NIH grant R01 AI41706, and R.M.L. is supported by NIH grant R01 GM62234.
PY - 2003/8/1
Y1 - 2003/8/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0041630781&partnerID=8YFLogxK
U2 - 10.1016/S0969-2126(03)00152-7
DO - 10.1016/S0969-2126(03)00152-7
M3 - Article
C2 - 12906833
AN - SCOPUS:0041630781
SN - 0969-2126
VL - 11
SP - 1025
EP - 1035
JO - Structure
JF - Structure
IS - 8
ER -