Reference: Müller CW and Schulz GE (1988) Structure of the complex of adenylate kinase from Escherichia coli with the inhibitor P1,P5-di(adenosine-5'-)pentaphosphate. J Mol Biol 202(4):909-12

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Abstract


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.

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Journal Article | Research Support, Non-U.S. Gov't
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Müller CW, Schulz GE
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