| Autor: |
Lunin, V.Yu, Levdikov, V.M, Shlyapnikov, S.V, Blagova, E.V, Lunin, V.V, Wilson, K.S, Mikhailov, A.M |
| Zdroj: |
FEBS Letters; July 1997, Vol. 412 Issue: 1 p217-222, 6p |
| Abstrakt: |
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 Smnuclease 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. |
| Databáze: |
Supplemental Index |
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