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3.1.31.1: micrococcal nuclease

This is an abbreviated version!
For detailed information about micrococcal nuclease, go to the full flat file.

Word Map on EC 3.1.31.1

Reaction

endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products =

Synonyms

AtTSN1, AtTSN2, cTSN, EC 3.1.4.7, Epstein-Barr virusencoded transcription factor 2 co-activator p100, HsTSN, micrococcal DNase, micrococcal endonuclease, Micrococcal nuclease, MN, MN ase, MNase, Nuc, NUC1, Nuc2, nucB, nuclease 8V, nuclease T, nuclease T', nuclease, micrococcal, nuclease, staphylococcal, NucM, P100, PaTSN, PfTSN, ribonucleate (deoxyribo-nucleate) 3'-nucleotidohydrolase, ribonucleate (deoxyribonucleate) 3'-nucleotidohydrolase, S. aureus nuclease, SNA, snake venom phosphodiesterase, SNase, SNAseR, SND1, spleen endonuclease, spleen phosphodiesterase, staph nuclease, staphylococcal nuclease, Staphylococcal nuclease A, Staphylococcal nuclease domain containing-1, staphylococcal nuclease domain-containing 1, staphylococcal nuclease domain-containing protein 1, staphylococcus aureus nuclease, staphylococcus aureus nuclease B, Staphylococcus aureus nuclease homologue, thermonuclease, TNase, TSN, tudor staphylococcal nuclease, Tudor-SN, Tudor-staphylococcal nuclease

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.31 Endoribonucleases that are active with either ribo- or deoxyribonucleic acids and produce 3'-phosphomonoesters
                3.1.31.1 micrococcal nuclease

Crystallization

Crystallization on EC 3.1.31.1 - micrococcal nuclease

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis, PDB ID 2SNS
crystal structure of binary Ca2+ and pdTp complexes of the D21E mutant enzyme
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three-dimensional diffuse x-ray scattering from crystals of the enzyme
x-ray structure
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crystals of the hyperstable mutant enzyme delta+PHS are grown using hanging drop vapor-diffusion methods at 4°C from a solution containing 17% 2-methyl-2,4-pentanediol, 2 M CaCl2, 3 M thymine-3',5'-diphosphate, and 25 mM potassium phosphate buffer, pH 8.0
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crystals of the I92E and I92K variant proteins are obtained at 4°C using the hanging-drop vapor-diffusion method
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E75A mutant: 4°C, hanging-drop, precipitating solution 37% (v/v) 2-methyl-2,4-pentanediol and 25 mM potassium phosphate buffer at pH 6.0, protein concentration 9.9 mg/ml before mixing with equal volume of precipitating solution. E75Q: 4°C, hanging-drop, precipitating solution 38% (v/v) 2-methyl-2,4-pentanediol and 25 mM potassium phosphate buffer at pH 6.0, starting from 14.2 mg/ml protein. Side chain of His121 is unaffected by elimination of Glu75, histidine moves closer to Glu101 in the structure with E75A. Both crystal structures suggest that the network of polar or ionizable groups connected through hydrogen bonding or charge-charge interactions is a rigid unit, incapable of reorganizing even when strongly stabilizing interactions between Glu75, His124, and Tyr93 are disrupted
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hanging drop vapor diffusion method
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LMYKGQPM, short peptide model from staphylococcal nuclease to model the conformational equilibrium between a hairpin conformation and its unfolded state (molecular dynamics simulation), in water, cubic model system, total simulation time 600 ns, starting from a polyproline II conformation, GROMOS96 force field under NVT conditions, 27°C: native and non-native hairpins are very close in free energies, interconversion can happen only through the unfolded conformation. Both folding and unfolding events display single exponential kinetics
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the V66K/P117G/H124L/S128A variant of nuclease is crystallized by the hanging drop vapor diffusion method at 4°C, 2 data sets are collected at -173.15°C, at pH 7 and 4.7, and the third is collected at 25.15°C and pH 5
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