@article{90aa9942d2a64027a0742e7b55d29676,
title = "Structure of the motor subunit of type I restriction-modification complex EcoR124I",
abstract = "Type I restriction-modification enzymes act as conventional adenine methylases on hemimethylated DNAs, but unmethylated recognition targets induce them to translocate thousands of base pairs before cleaving distant sites nonspecifically. The first crystal structure of a type I motor subunit responsible for translocation and cleavage suggests how the pentameric translocating complex is assembled and provides a structural framework for translocation of duplex DNA by RecA-like ATPase motors.",
author = "Mikalai Lapkouski and Santosh Panjikar and Pavel Janscak and Smatanova, {Ivana Kuta} and Jannette Carey and R{\"u}diger Ettrich and Eva Csefalvay",
note = "Funding Information: We gratefully acknowledge support from the Ministry of Education, Youth and Sports of the Czech Republic (MSM6007665808, LC06010), Academy of Sciences of the Czech Republic (AVOZ60870520), Grant Agency of the Czech Republic (203/08/0114 to R.E), the European Molecular Biology Organization (to M.L.), the Swiss National Science Foundation (to P.J.) and joint Czech and US National Science Foundation International Research Cooperation (INT03-09049 to J.C.). We thank the European Molecular Biology Laboratory for access to the X12 beamline at the DORIS storage ring, DESY, Hamburg. J.C. and R.E. thank F. Hughson, T. Lohman, B. Matthews, L. Raleigh and S. Weller for insightful discussion during preparation of the manuscript.",
year = "2009",
month = jan,
doi = "10.1038/nsmb.1523",
language = "English (US)",
volume = "16",
pages = "94--95",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "Nature Publishing Group",
number = "1",
}