Three‐dimensional structure of Serratia marcescens nuclease at 1.7 Å resolution and mechanism of its action

FEBS Letters

Levdikov, V.M²  Mikhailov, A.M²  Lunin, V.V¹  Lunin, V.Yu⁴  Shlyapnikov, S.V⁵  Wilson, K.S³  Blagova, E.V² 

[1] Chemical Department, Moscow State University, 119899 Moscow, Russia;Institute of Crystallography, Russian Academy of Sciences, Leninsky pr. 59, 117333 Moscow, Russia;European Molecular Biology Laboratory, c/o DESY, 2000 Hamburg 52, Germany;Institute of Mathematical Problems in Biology, Russian Academy of Sciences, 142292 Pushino, Moscow region, Russia;Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, 117984 Moscow, Russia

关键词: Serratia marcescens;    Endonuclease;    X-ray structure;    Sequence analysis;    Catalytic mechanism;    Sm nuclease;    endonuclease of Serratia marcescens (EC 3.1.4.9);   

DOI  :  10.1016/S0014-5793(97)00512-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown