Structure of the complex of adenylate kinase from Escherichia coli with the inhibitor P1,P5-di(adenosine-5'-)pentaphosphate.
The enzyme adenylate kinase was isolated from Escherichia coli and crystallized together with a substrate-mimicking inhibitor. The crystal structure was solved using the multiple isomorphous replacement method at a resolution of 4.5 A (1 A = 0.1 nm). There are two enzyme-inhibitor complex molecules in the asymmetric unit, the relative positions of which are given. The resolution was extended to 2.3 A starting with the model of the homologous enzyme from yeast and using constrained-restrained and restrained refinements together with the known non-crystallographic symmetry. The final R-factor is 35.9%. The corresponding model is given as backbone tracing. The structure will be used for protein-engineering studies.
Müller
C W
CW
Institut für Organische Chemie und Biochemie der Universität, Freiburg i.Br., F.R.G.
Schulz
G E
GE
D000263:Adenylate Kinase / Q000037:antagonists & inhibitors*; D015226:Dinucleoside Phosphates / Q000494:pharmacology*; D004926:Escherichia coli / Q000201:enzymology; D008958:Models, Molecular; D010770:Phosphotransferases / Q000037:antagonists & inhibitors*; D014961:X-Ray Diffraction
D015226:Dinucleoside Phosphates; C012276:diadenosine pyrophosphate; D010770:Phosphotransferases; D000263:Adenylate Kinase