[Conformation of aspartate aminotransferase in crystals].
X-ray study of chicken cytosolic aspartate aminotransferase revealed conformational changes in the protein of two kinds: (1) a shift of the small domain adjacent to substrate-binding area due to interaction of the protein with two carboxyl groups of substrate and (2) a change in inclination of the coenzyme plane due to replacement of C = N bond of the coenzyme with Lys-258 by C = N bond with a substrate. An asymmetry in subunit behaviour is observed in both cases: the domain is shifted in one subunit and the coenzyme is rotated in other. Substrate-binding properties of each subunit are strictly dependent on the protein conformation in substrate-binding area.
D000818:Animals; D001219:Aspartate Aminotransferases / Q000378:metabolism*; D002645:Chickens; D003460:Crystallization; D003600:Cytosol / Q000201:enzymology; D008928:Mitochondria / Q000201:enzymology; D008958:Models, Molecular; D011487:Protein Conformation; D014961:X-Ray Diffraction
D001219:Aspartate Aminotransferases
Konformatsii aspartataminotransferazy v kristalle.