Structure of the motor subunit of type I restriction-modification complex EcoR124I.
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.
Lapkouski
Mikalai
M
Department of Structure and Function of Proteins, Institute of Systems Biology and Ecology, Academy of Sciences of the Czech Republic, Nove Hrady, Czech Republic.
Panjikar
Santosh
S
Janscak
Pavel
P
Smatanova
Ivana Kuta
IK
Carey
Jannette
J
Ettrich
Rüdiger
R
Csefalvay
Eva
E
D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D015253:Deoxyribonucleases, Type I Site-Specific / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism
D021122:Protein Subunits; D000255:Adenosine Triphosphate; C048242:endodeoxyribonuclease EcoR124I; D015253:Deoxyribonucleases, Type I Site-Specific