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

V Y  Lunin; V M  Levdikov; S V  Shlyapnikov; E V  Blagova; V V  Lunin; K S  Wilson; A M  Mikhailov

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

V Y Lunin, V M Levdikov, S V Shlyapnikov, E V Blagova, V V Lunin, K S Wilson, A M Mikhailov

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

The three-dimensional crystal structure of Serratia marcescens (Sm) nuclease has been refined at 1.7 Angstrom 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. (C) 1997 Federation of European Biochemical Societies.

Original language	English
Pages (from-to)	217-222
Number of pages	6
Journal	FEBS Letters
Volume	412
Issue number	1
Publication status	Published - 21 Jul 1997

Cite this

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title = "Three-dimensional structure of Serratia marcescens nuclease at 1.7 {\AA} resolution and mechanism of its action",

abstract = "The three-dimensional crystal structure of Serratia marcescens (Sm) nuclease has been refined at 1.7 Angstrom 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. (C) 1997 Federation of European Biochemical Societies.",

author = "Lunin, {V Y} and Levdikov, {V M} and Shlyapnikov, {S V} and Blagova, {E V} and Lunin, {V V} and Wilson, {K S} and Mikhailov, {A M}",

year = "1997",

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day = "21",

language = "English",

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pages = "217--222",

journal = "FEBS Letters",

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T1 - Three-dimensional structure of Serratia marcescens nuclease at 1.7 Å resolution and mechanism of its action

AU - Lunin, V Y

AU - Levdikov, V M

AU - Shlyapnikov, S V

AU - Blagova, E V

AU - Lunin, V V

AU - Wilson, K S

AU - Mikhailov, A M

PY - 1997/7/21

Y1 - 1997/7/21

N2 - The three-dimensional crystal structure of Serratia marcescens (Sm) nuclease has been refined at 1.7 Angstrom 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. (C) 1997 Federation of European Biochemical Societies.

AB - The three-dimensional crystal structure of Serratia marcescens (Sm) nuclease has been refined at 1.7 Angstrom 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. (C) 1997 Federation of European Biochemical Societies.

M3 - Article

SN - 0014-5793

VL - 412

SP - 217

EP - 222

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -