title: The elastic network model reveals a consistent picture on intrinsic functional dynamics of type II restriction endonucleases.
abstract: The vibrational dynamics of various type II restriction endonucleases, in complex with cognate/non-cognate DNA and in the apo form, are investigated with the elastic network model in order to reveal common functional mechanisms in this enzyme family. Scissor-like and tong-like motions observed in the slowest modes of all enzymes and their complexes point to common DNA recognition and cleavage mechanisms. Normal mode analysis further points out that the scissor-like motion has an important role in differentiating between cognate and non-cognate sequences at the recognition site, thus implying its catalytic relevance. Flexible regions observed around the DNA-binding site of the enzyme usually concentrate on the highly conserved β-strands, especially after DNA binding. These β-strands may have a structurally stabilizing role in functional dynamics for target site recognition and cleavage. In addition, hot spot residues based on high-frequency modes reveal possible communication pathways between the two distant cleavage sites in the enzyme family. Some of these hot spots also exist on the shortest path between the catalytic sites and are highly conserved.
authors.affiliation: Department of Chemical Engineering and Polymer Research Center, Bogazici University, 34342 Bebek, Istanbul, Turkey.
authors.forename: A
authors.initials: A
authors.lastname: Uyar
authors.forename: O
authors.initials: O
authors.lastname: Kurkcuoglu
authors.forename: L
authors.initials: L
authors.lastname: Nilsson
authors.forename: P
authors.initials: P
authors.lastname: Doruker
mesh_terms: D001665:Binding Sites; D020134:Catalytic Domain; D004247:DNA / Q000737:chemistry; D015252:Deoxyribonucleases, Type II Site-Specific / Q000737:chemistry*; D008958:Models, Molecular; D016571:Neural Networks, Computer; D011487:Protein Conformation
chemical_list: D004247:DNA; D015252:Deoxyribonucleases, Type II Site-Specific