Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of an archaeal alanine:glyoxylate aminotransferase.,Sakuraba H, Yoneda K, Takeuchi K, Tsuge H, Katunuma N, Ohshima T Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):696-9. Epub 2008 May 14. PMID:18560158[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sakuraba H, Yoneda K, Takeuchi K, Tsuge H, Katunuma N, Ohshima T. Structure of an archaeal alanine:glyoxylate aminotransferase. Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):696-9. Epub 2008 May 14. PMID:18560158 doi:10.1107/S0907444908006732
