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Three‐dimensional structure of Serratia marcescens nuclease at 1.7 Å resolution and mechanism of its action
Author(s) -
Lunin V.Yu,
Levdikov V.M,
Shlyapnikov S.V,
Blagova E.V,
Lunin V.V,
Wilson K.S,
Mikhailov A.M
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00512-7
Subject(s) - serratia marcescens , nuclease , chemistry , monomer , stereochemistry , crystallography , molecule , resolution (logic) , hydrogen bond , mechanism of action , enzyme , biochemistry , escherichia coli , organic chemistry , artificial intelligence , computer science , gene , polymer , in vitro
The three‐dimensional crystal structure of Serratia marcescens ( Sm ) nuclease has been refined at 1.7 Å resolution to the R‐factor of 17.3% and R‐free of 22.2%. The final model consists of 3678 non‐hydrogen atoms and 443 water molecules. The analysis of the secondary and the tertiary structures of the Sm nuclease suggests a topology which reveals essential inner symmetry in all the three layers forming the monomer. We propose the plausible mechanism of its action based on a concerted participation of the catalytically important amino acid residues of the enzyme active site.