EC Number   |
|---|
   3.6.1.71 | aprataxin forkhead-associated domain and modeling of the pSDpTD peptide into the apo structure. pT recognition is provided by residues Arg29 and Ser41 |
| 3.6.1.71 | crystal structure in complex with GMP, to 1.5 A resolution. GMP binds at the same position and in the same anti nucleoside conformation as AMP, and aprataxin makes more extensive nucleobase contacts with guanine than with adenine, via a hydrogen bonding network to the guanine O6, N1, N2 base edge |
| 3.6.1.71 | purified wild-type enzyme in complex with RNA/DNA, hAPTX-nicked-RNA-DNA-AMP-Zn2+ complex is grown by mixing 300 nl of 10 mg/ml hAptx (165-342) protein and 1 mM AMP, 1.5:1 DNA:protein molar ratio, in 150 mM NaCl, 20 mM Tris-HCl, pH 7.5, and 0.1% 2-mercaptoethanol, with an equal volume of precipitant solution containing 100 mM MES, pH 6.5, 16% w/v PEG 3350 at 4°C, methods for mutant product complexes hAPTX-R199H/RNA-DNA/AMP-Zn2+, hAPTXH201Q/RNA-DNA/AMP-Zn2+, hAPTX-S242N/RNA-DNA/AMPZn2+, hAPTX-L248M/DNA/AMP-Zn2+, and hAPTX-V263G/RNA-DNA/AMP-Zn2+, differ, overview. X-ray diffraction structure determination and analysis, molecular replacement using PDB ID 4NDG as a search model |
| 3.6.1.71 | structure of APTX in complex with DNA, AMP and Zn2+ reveals active site and DNA interaction clefts formed by fusing a histidine triad nucleotide hydrolase with an DNA minor groove binding C2HE Zn-finger. An Aptx helical wedge interrogates the base stack for DNA end/nick sensing. Histidine triad nucleotide hydrolase, Zn-finger, the wedge, and an [F/Y]PK pivot motif cooperate to distort terminal DNA base-pairing and direct 5'-AMP into the active site pocket |
| 3.6.1.71 | structure-function studies of human Aptx in complex with RNA-DNA, AMP and Zn2+ |
| 3.6.1.71 | structures of apo form and in complex with dsDNA and dsDNA-AMP. The bound DNA adopts a 5'-flap conformation that facilitates 5'-AMP access to the active site, where AMP cleavage occurs by a canonical catalytic mechanism |
| 3.6.1.71 | structures of aprataxin Hnt3 in its apo form and in complex with dsDNA and dsDNA-AMP. The bound DNA adopts a 5'-flap conformation that facilitates 5'-AMP access to the active site, where AMP cleavage occurs by a canonical catalytic mechanism |
