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Five‐stranded β‐sheet sandwiched with two α‐helices: A structural link between restriction endonucleases Eco RI and Eco RV
Author(s) -
Venclovas Česlovas,
Timinskas Albertas,
Siksnys Virginijus
Publication year - 1994
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340200308
Subject(s) - ecorv , ecori , restriction enzyme , beta sheet , dna , peptide sequence , chemistry , alpha helix , crystallography , protein structure , stereochemistry , biology , biochemistry , gene
Examination of crystal structures of restriction endonucleases Eco RI and Eco RV complexes with their cognate DNA revealed a common structural element, which forms the core of both proteins. This element consists of a five‐stranded β‐sheet and two α‐helices packed against it and could be described as α–β sandwich in which helices and β‐strands lie in two stacked layers. While the spatial structure of this α–β sandwich is conserved in both enzymes, there are no detectable similarities between amino acid sequences except of a few residues involved in active site formation. Probably, other restriction endonucleases which have similar organization of the active site might possess similar structural element regardless of DNA sequence recognized and recognition elements in the enzyme used. © 1994 Wiley‐Liss, Inc.