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4.6.1.16: tRNA-intron lyase

This is an abbreviated version!
For detailed information about tRNA-intron lyase, go to the full flat file.

Word Map on EC 4.6.1.16

Reaction

pretRNA
=
a 3'-half-tRNA molecule with a 5'-OH end
 +
a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end
 +
an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus

Synonyms

AF endonuclease, AFN, AF_0900, archaeal pre-tRNA splicing endonuclease, ARMAN-2 EndA, EC 3.1.27.9, EndA, EndATa, epsilon2 endonuclease, Gamma-toxin, hClp1, HEAB, homing endonuclease, HSPC117, I-TevI, intron-encoded endonuclease, MJ1424, More, nuclease, transfer ribonucleate intron endoribo-, pre-tRNA splicing endonuclease, RNA splicing endonuclease, RNA-splicing endonuclease, Sen2, splicing endonuclease, ssol_1416, STK_03580, three-unit tRNA splicing endonuclease, transfer ribonucleate intron endoribonuclease, transfer splicing endonuclease, tRNA anticodon nucleases (ACNs), tRNA endonuclease, tRNA intron endonuclease, tRNA intron-splicing endonuclease, tRNA SEN, tRNA splicing endonuclease, tRNA splicing ligase, tRNA-intron endonuclease, tRNA-splicing endonuclease, tRNATRPintron endonuclease

ECTree

     4 Lyases
         4.6 Phosphorus-oxygen lyases
             4.6.1 Phosphorus-oxygen lyases (only sub-subclass identified to date)
                4.6.1.16 tRNA-intron lyase

Crystallization

Crystallization on EC 4.6.1.16 - tRNA-intron lyase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and mutant APE-EndAs, hanging-drop vapor diffusion method, 10 mg/ml protein solution is mixed in equal volumes with reservoir solution containing 0.25 M ammonium sulfate, 0.1 M sodium citrate, pH 5.6, 0.9 M lithium sulfate and 1 mM MgCl2, 1 day, equilibration over 0.5 ml reservoir solution, 22°C, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement
purified recombinant wild-type and mutant EndAs, method screening, sitting drop vapor diffusion technique, mixing of 0.001 ml protein solution with 0.001 ml reservoir solution containing 0.2 M NaCl, 0.1 M phosphate-citrate, pH 4.2, and 10% w/v PEG 3000, equilibration over 0.1 ml reservoir solution, 22°C, X-ray diffraction structure determmination and analysis at 1.7-2.3 A resolution, molecular replacement
purified recombinant AFU-EndA, hanging-drop vapor diffusion method, 10 mg/ml protein solution is mixed in equal volumes with reservoir solution containing 2.2 M ammonium sulfate, 0.2 M potassium sodium tartrate tetrahydrate and 0.1 M sodium citrate, pH 5.6, several days, equilibration over 0.5 ml reservoir solution, 22°C, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement
-
truncated active dimeric enzyme form lacking the N-terminal domain, hanging drop vapour diffusion method, 60 mg/ml protein is mixed with reservoir solution conatining 0.1 M sodium cacodylate, pH 6.5-6.8, 20 mM ammonium sulfate, and 0.3-0.4 M sodium acetate, approximately 30 days, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
hanging-drop vapor diffusion method
catalytic subunit, X-ray diffraction structure determination and analysis at 3.1 A resolution
-
Crystallization was performed at 44°C by the sitting-drop method using a Hydra II Plus One crystallization robot (Matrix Technology) with approximately 1500 conditions and a ratio of 200 nl precipitants to 200 nl protein solution.