Structural highlights
FunctionT2A1_THAGE Recognizes the double-stranded sequence ACCGGT and cleaves after A-1. Publication Abstract from PubMedAlthough all Type II restriction endonucleases catalyze phosphodiester bond hydrolysis within or close to their DNA target sites, they form different oligomeric assemblies ranging from monomers, dimers, tetramers to higher order oligomers to generate a double strand break in DNA. Type IIP restriction endonuclease AgeI recognizes a palindromic sequence 5'-A/CCGGT-3' and cuts it ('/' denotes the cleavage site) producing staggered DNA ends. Here, we present crystal structures of AgeI in apo and DNA-bound forms. The structure of AgeI is similar to the restriction enzymes that share in their target sites a conserved CCGG tetranucleotide and a cleavage pattern. Structure analysis and biochemical data indicate, that AgeI is a monomer in the apo-form both in the crystal and in solution, however, it binds and cleaves the palindromic target site as a dimer. DNA cleavage mechanism of AgeI is novel among Type IIP restriction endonucleases. Restriction endonuclease AgeI is a monomer which dimerizes to cleave DNA.,Tamulaitiene G, Jovaisaite V, Tamulaitis G, Songailiene I, Manakova E, Zaremba M, Grazulis S, Xu SY, Siksnys V Nucleic Acids Res. 2016 Dec 29. pii: gkw1310. doi: 10.1093/nar/gkw1310. PMID:28039325[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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