Alternative arrangements of catalytic residues at the active sites of restriction enzymes
Copyright policy )Alternative arrangements of catalytic residues at the active sites of restriction enzymes
A catalytic sequence motif PDX10–30(E/D)XK is found in many restriction enzymes. On the basis of sequence similarities and mapping of the conserved residues to the crystal structure of NgoMIV we suggest that residues D160, K182, R186, R188 and E195 contribute to the catalytic/DNA binding site of the Ecl18kI restriction endonuclease. Mutational analysis confirms the functional significance of the conserved residues of Ecl18kI. Therefore, we conclude that the active site motif 159VDX21KX12E of Ecl18kI differs from the canonical PDX10–30(E/D)XK motif characteristic for most of the restriction enzymes. Moreover, we propose that two subfamilies of endonucleases Ecl18kI/PspGI/EcoRII and Cfr10I/Bse634I/NgoMIV, specific, respectively, for CCNGG/CCWGG and RCCGGY/GCCGGC sites, share conserved active site architecture and DNA binding elements.
- Russian Academy of Sciences Russian Federation
- Russian Academy of Science Russian Federation
- Institute of Biochemistry and Physiology of Microorganisms Russian Federation
- Department of Biological Sciences Russian Federation
Models, Molecular, Binding Sites, Base Sequence, Active site, Restriction endonuclease Ecl18kI, Amino Acid Motifs, Molecular Sequence Data, DNA, Mutagenesis, Catalytic Domain, Mutation, Animals, Amino Acid Sequence, Amino Acids, Deoxyribonucleases, Type II Site-Specific, Sequence Alignment, Conserved Sequence
Models, Molecular, Binding Sites, Base Sequence, Active site, Restriction endonuclease Ecl18kI, Amino Acid Motifs, Molecular Sequence Data, DNA, Mutagenesis, Catalytic Domain, Mutation, Animals, Amino Acid Sequence, Amino Acids, Deoxyribonucleases, Type II Site-Specific, Sequence Alignment, Conserved Sequence
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