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Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase

Nature Structural Biology volume 8, pages 423–426 (2001)Cite this article

Abstract

Regulation of protein function, often achieved by allosteric mechanisms, is central to normal physiology and cellular processes. Although numerous models have been proposed to account for the cooperative binding of ligands to allosteric proteins and enzymes, direct structural support has been lacking. Here, we used a combination of X-ray crystallography and small angle X-ray scattering in solution to provide direct structural evidence that the binding of ligand to just one of the six active sites of Escherichia coli aspartate transcarbamoylase induces a concerted structural transition from the T to the R state.

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Figure 1: The T and R states of ATCase and stereo view of the active site of ATCase.
Figure 2: Small-angle X-ray scattering.
Figure 3: Hybrid enzyme formation and purification.

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Acknowledgements

This work was supported by the National Institute of General Medical Sciences. The Stanford Synchrotron Radiation Laboratory (SSRL) is operated by the Department of Energy, Office of Basic Energy Sciences. The SSRL Structural Biology Resource is supported by the National Institutes of Health, National Center for Research Resources and by the Department of Energy, Office of Biological and Environmental Research.

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Authors and Affiliations

  1. Department of Chemistry, Boston College, Merkert Chemistry Center, Chestnut Hill, 02467, Massachusetts, USA

    Christine P. Macol & Evan R. Kantrowitz

  2. Stanford Synchrotron Radiation Laboratory, SLAC, P.O. Box 4349, MS69, Stanford, 94309-0210, California, USA

    Hiro Tsuruta

  3. Department of Biochemistry and Cell Biology, W. M. Keck Center for Computational Biology, Rice University, Houston, 77005, Texas, USA

    Boguslaw Stec

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  1. Christine P. Macol
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  2. Hiro Tsuruta
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  4. Evan R. Kantrowitz
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Correspondence to Evan R. Kantrowitz.

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Macol, C., Tsuruta, H., Stec, B. et al. Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase. Nat Struct Mol Biol 8, 423–426 (2001). https://doi.org/10.1038/87582

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