2W00

Crystal structure of the HsdR subunit of the EcoR124I restriction enzyme in complex with ATP

Summary for 2W00

• Entry DOI: 10.2210/pdb2w00/pdb
• Descriptor: HSDR, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: atp-binding, dna-binding, restriction system, helicase, hydrolase, r.ecor124i, nucleotide-binding, type i restriction-modification enzyme
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 2
• Total formula weight: 243027.63

Authors

Lapkouski, M.,Panjikar, S.,Kuta Smatanova, I.,Ettrich, R.,Csefalvay, E. (deposition date: 2008-08-08, release date: 2008-12-16, Last modification date: 2024-10-16)

Primary citation

Lapkouski, M.,Panjikar, S.,Janscak, P.,Smatanova, I.K.,Carey, J.,Ettrich, R.,Csefalvay, E.
Structure of the Motor Subunit of Type I Restriction-Modification Complex Ecor124I.
Nat.Struct.Mol.Biol., 16:94-, 2009

PubMed 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.

PubMed: 19079266
DOI: 10.1038/NSMB.1523

Experimental method

X-RAY DIFFRACTION (2.6 Å)