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3.1.11.1: exodeoxyribonuclease I

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

Word Map on EC 3.1.11.1

Reaction

Exonucleolytic cleavage in the 3'- to 5'- direction to yield nucleoside 5'-phosphates =

Synonyms

3'->5'exonuclease, 3'-to-5' exonuclease, 3'5' exonuclease, 30–50 ssExo, DNA deoxyribophosphodiesterase, DNA polymerase D, DNA polymerase I, dRPase, E. coli exonuclease I, EC 3.1.4.25, Escherichia coli exonuclease I, Exo I, Exo1, EXO1b, ExoA, ExoI, exonuclease 1, exonuclease 1b, exonuclease I, exonuxlease 1, hEXO1, More, OsEXO1, PF2046, PfuExo I, PhoExo I, phosphodiesterase, Pol, Pol BI, POlB1, polD, SbcB15, single-strand DNA 3'-5' exonuclease, single-strand-specific 3'-5' exonuclease, single-stranded DNA-specific 3'-5' exonuclease I, Sso polB1, SSO0552, tthb178, WRN

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.11 Exodeoxyribonucleases producing 5′-phosphomonoesters
                3.1.11.1 exodeoxyribonuclease I

Crystallization

Crystallization on EC 3.1.11.1 - exodeoxyribonuclease I

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 16% (w/v) PEG 4000, 0.1 M Tris pH 8.5, 0.2 M CaCl2
by hanging-drop vapor-diffusion method, unbound ExoI, to 1.7 resolution. ExoI bound to the C terminus of ssDNA-binding protein, at 2.7 A resolution. Two C terminus ssDNA-binding proteins bind to adjacent sites on ExoI
hanging-drop vapour-diffusion method at room temperature, structure of ExoI in complex with a nucleotide product, thymidine 5'-monophosphate
in complex with thymidine 5'-monophosphate, hanging drop vapour diffusion method, using 200 mM NaCl, 100 mM Tris-HCl pH 8.5, and 20% (w/v) PEG 8000
purified enzyme in complex with four different ssDNA substrates, 5'-Cy5-dT13, 5'-Cy5-dA13, dA16 and dT13, hanging drop vapor diffusion, 0.002 ml of 10 mg/ml enzyme in 20 mM Tris, 1 mM DTT, 10 mM EDTA, pH 8.0, with a 1.2 molar excess of oligonucleotide, is mixed with 0.002 ml of reservoir solution containing 0.9-1.5M ammonium sulfate, 3.75–6.0% 2-propanol and 25% glycerol, 1 week, X-ray diffraction structure determination and analysis at 2.0-3.7 A resolution
X-ray structure determination
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crystallization of recombinant wild-type native and selenomethionine-labeled enzyme, and of recombinant mutant D173A enzyme in complex with metal ions, X-ray diffraction structure determination and analysis at 2.5-3.4 A resolution, modelling
solubilization of the inclusion bodies is performed by the high-pressure refolding method and highly purified protein is subjected to crystallization by the sitting-drop vapour-diffusion method at 20°C. A crystal of PhoExo I is obtained in a reservoir solution consisting of 0.1 M Tris-HCl pH 8.9, 27% PEG 6000 and diffracts X-rays to 1.52 A resolution. The crystal of PhoExo I belong to space group H32, with unit-cell parameters a = b = 112.07, c = 202.28 A. The crystal contains two PhoExo I molecules in the asymmetric unit
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