Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase.
X-ray diffraction studies to 2.8-A resolution have yielded the three-dimensional structure of mitochondrial aspartate aminotransferase (L-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1), an isologous alpha 2 dimer (Mr = 2 x 45,000). The subunits are rich in secondary structure and contain two domains, one of which anchors the coenzyme, pyridoxal 5'-phosphate. Each active site lies between the subunits and is composed of residues from both of them.
D000818:Animals; D001219:Aspartate Aminotransferases / Q000378:metabolism; D001665:Binding Sites; D002645:Chickens; D006860:Hydrogen Bonding; D046911:Macromolecular Substances; D008928:Mitochondria / Q000201:enzymology*; D008958:Models, Molecular; D011487:Protein Conformation; D011732:Pyridoxal Phosphate / Q000378:metabolism; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D011732:Pyridoxal Phosphate; D001219:Aspartate Aminotransferases