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Journal Article

Three-dimensional structure of adenyl kinase

MPS-Authors
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Schulz,  G. E.
Max Planck Institute for Medical Research, Max Planck Society;

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Elzinga,  M.
Max Planck Institute for Medical Research, Max Planck Society;

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Marx,  F.
Max Planck Institute for Medical Research, Max Planck Society;

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Schirmer,  R. Heiner
Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Schulz, G. E., Elzinga, M., Marx, F., & Schirmer, R. H. (1974). Three-dimensional structure of adenyl kinase. Nature, 250, 120-123. doi:10.1038/250120a0.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-DC9E-A
Abstract
A combination of X-ray data at 3 Å resolution and sequence results has yielded the atomic structure of adenyl kinase, a ubiquitous enzyme which catalyses the phosphorylation of AMP by ATP. The abundant secondary structures of the protein and the probable binding sites for ATP and AMP are described.