The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 A resolution.
The crystal structure of the complex between adenylate kinase from bovine mitochondrial matrix and its substrate AMP has been refined at 1.85 A resolution (1 A = 0.1 nm). Based on 42,519 independent reflections of better than 10 A resolution, a final R-factor of 18.9% was obtained with a model obeying standard geometry within 0.016 A in bond lengths and 3.2 degrees in bond angles. There are two enzyme: substrate complexes in the asymmetric unit, each consisting of 226 amino acid residues, one AMP and one sulfate ion. A superposition of the two full-length polypeptides revealed deviations that can be described as small relative movements of three domains. Best superpositions of individual domains yielded a residual overall root-mean-square deviation of 0.3 A for the backbone atoms and 0.5 A for the sidechains. The final model contains 381 solvent molecules in the asymmetric unit, 2 x 72 = 144 of which occupy corresponding positions in both complexes.
Diederichs
K
K
Institut für Organische Chemie und Biochemie Freiburg, F.R.G.
Schulz
G E
GE
D000249:Adenosine Monophosphate / Q000378:metabolism*; D000263:Adenylate Kinase / Q000648:ultrastructure*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003461:Crystallography; D006860:Hydrogen Bonding; D008929:Mitochondria, Heart / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012997:Solvents; D013696:Temperature; D014961:X-Ray Diffraction
D012997:Solvents; D000249:Adenosine Monophosphate; D000263:Adenylate Kinase