2ZC0
Crystal structure of an archaeal alanine:glyoxylate aminotransferase
Summary for 2ZC0
| Entry DOI | 10.2210/pdb2zc0/pdb |
| Descriptor | Alanine glyoxylate transaminase, ZINC ION, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, ... (5 entities in total) |
| Functional Keywords | alanine:glyoxylate aminotransferase, archaea, thermococcus litoralis, transferase |
| Biological source | Thermococcus litoralis |
| Total number of polymer chains | 4 |
| Total formula weight | 182441.39 |
| Authors | Sakuraba, H.,Yoneda, K.,Tsuge, H.,Ohshima, T. (deposition date: 2007-10-31, release date: 2008-06-17, Last modification date: 2024-03-13) |
| Primary citation | Sakuraba, H.,Yoneda, K.,Takeuchi, K.,Tsuge, H.,Katunuma, N.,Ohshima, T. Structure of an archaeal alanine:glyoxylate aminotransferase Acta Crystallogr.,Sect.D, 64:696-699, 2008 Cited by PubMed Abstract: The crystal structure of a novel alanine:glyoxylate aminotransferase from the hyperthermophilic archaeon Thermococcus litoralis was determined at 2.3 A resolution. The asymmetric unit contains four homologous subunits and the functional tetramer is generated by noncrystallographic 222 symmetry. Although the main-chain coordinates of the monomer of the Thermococcus litoralis enzyme showed a high degree of similarity to those of aspartate aminotransferase from Thermus thermophilus HB8, the amino-acid residues involved in substrate binding in the aspartate aminotransferase are only partially conserved in the Thermococcus litoralis enzyme. This may account for the difference in the substrate specificities of the two enzymes. PubMed: 18560158DOI: 10.1107/S0907444908006732 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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