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3.1.11.5: exodeoxyribonuclease V

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

Word Map on EC 3.1.11.5

Reaction

Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides =

Synonyms

AddAB enzyme, E. coli ATP-dependent DNase, E. coli exonuclease V, Escherichia coli exonuclease V, Escherichia coli RecBCD, Exodeoxyribonuclease V 125 kDa polypeptide, Exodeoxyribonuclease V 135 KDA polypeptide, Exodeoxyribonuclease V 67 kDa polypeptide, exonuclease V, ExoV, gene recBC DNase, gene RecBC endoenzyme, nuclease, exodeoxyribo V, PAB2263, RecB, RecB helicase-nuclease, REcB30 protein, recBC deoxyribonuclease, recBC DNase, recBC nuclease, RecBCD, RecBCD DNase, recBCD enzyme, RecBCD exonuclease, RecBCD-type helicase-nuclease, RecD, UPF0286 protein PYRAB01260

ECTree

     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.11 Exodeoxyribonucleases producing 5′-phosphomonoesters
                3.1.11.5 exodeoxyribonuclease V

Crystallization

Crystallization on EC 3.1.11.5 - exodeoxyribonuclease V

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme complex RecBCD bound with a DNA substrate (a 350 kDa complex) or ATP analogue ADPNP, mixing of 0.0015 ml of 5 mg/ml protein, and a 1.75fold excess of DNA, 2 mM ADPNP, and 4 mM MgCl2, in 20 mM Tris-HCl, pH 7.5, 50 mM NaCl, and 1 mM TCEP, with 0.03 ml of 0.1% detergent n-dodecyl beta-D-maltoside on ice, incubation at 4°C overnight, X-ray diffraction structure determination and analysis at 3.8 A resolution, molecular replacement and modelling using the crystal structure of RecBCD in complex with an extended DNA fork (PDB ID 3K70) as a template
vapour-diffusion hanging drop method, crystal structure of a complex of Escherichia coli RecBCD enzyme bound to ablunt-ended DNA hairpin
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crystallisation of a Rec-B like nuclease by the sitting-drop vapour-diffusion method using polyethylene glycol 8000 as the precipitant. The crystals belong to the orthorhombic space group C222(1), with unit-cell parameters a = 81.5, b= 159.8, c = 100.8 A. There is a dimer in the asymmetric unit with its local twofold axis running parallel to the crystallographic twofold screw axis. The crystals diffract to about 2 A and a complete native data set is collected to 2.65 A resolution