EC Number   |
Reference |
|---|
    6.1.1.7 | 453 amino acid catalytic fragment Aa-AlaRS453 |
662825 |
| 6.1.1.7 | AlaRS-DELTAC, comprising the aminoacylation, tRNA-recognition, and editing domains, and AlaRS-C, comprising the dimerization domain. The aminoacylation/tRNA-recognition domains contain an insertion incompatible with the class-specific tRNA-binding mode. The editing domain is fixed tightly via hydrophobic interactions to the aminoacylation/tRNA-recognition domains, on the side opposite from that in threonyl-tRNA synthetase. A groove formed between the aminoacylation/tRNA-recognition domains and the editing domain appears to be an alternative tRNA-binding site. The amino acid residues required for the G3:U70 base pair recognition are mapped in this groove. The dimerization domain consists of helical and globular subdomains. The helical subdomain mediates dimerization by forming a helixloophelix zipper. The globular subdomain, which is important for the aminoacylation and editing activities, has a positively-charged face suitable for tRNA binding |
706543 |
| 6.1.1.7 | cocrystal structures with Mg2+-ATP, L-alanine, glycine and L-serine with each separately |
663256 |
| 6.1.1.7 | molecular replacement with the apo-AlaRS structure from Aquifex aeolicus,Protein Data Bank accession code 1RIQ, as the initial model |
705890 |
| 6.1.1.7 | monomer structures of C-terminally truncated AlaRS, with both activation and editing domains in the apo form, in complex with an Ala-AMP analog, and in a high-resolution lysine-methylated form. Docking of the editing domain to the activation domain occurs opposite from the predicted tRNA-binding surface. The editing site is positioned more than 35 A from the activation site. Results suggest that tRNA translocation via a canonical CCA flipping is unlikely to occur in AlaRS. Zinc binds in the editing site, in which the specific coordination of zinc will be facilitated by a conserved GGQ motif |
706502 |
| 6.1.1.7 | of small fragments |
511 |
| 6.1.1.7 | purified recombinant appended C-terminal domain (C-Ala), two different crystal forms, each of which is specific to a particular condition are achieved, one of these crystal forms harbors the monomer and is obtained using 0.1 M Tris, pH 8.5, and 25% w/v PEG 3350, whereas the other captures a dimer using 0.2 M ammonium acetate, 0.1 M Tris, pH 8.5, and 25% w/v PEG 3350, X-ray diffraction structure determination and analysis |
746308 |
| 6.1.1.7 | purified recombinant full-length enzyme, N-terminal domain, and C-terminal domain, hanging-drop vapour-diffusion method, mixing of 0.001 ml of protein and reservoir solution, and equilibration against 0.5 ml of reservoir solution at 20°C, for crystallization of the AlaRS-FLtRNAAla complex, tRNAAla is heated at 80°C for 5 min and is gradually cooled to room temperature for refolding, in presence of 1 mM AMP-PNP, different methods for the different protein samples are used, overview, X-ray diffraction structure determination and analysis at 3.2-3.5 A resolution |
671126 |
| 6.1.1.7 | purified recombinant wild-type and selenomethionine-labeld AlaRS editing-domain homolog, PH0574, 37.6 mg/ml protein, 27.5%w/v PEG 4000, and 100 mM MES-Na, pH 6.3, using a full-automatic protein crystallization and observation system, X-ray diffraction structure determination and analysis at 1.45 A resolution |
677045 |
