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Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme

Nature Structural Biology volume 7, pages 555–559 (2000)Cite this article

Abstract

Here we report the solution and refinement at 1.9 Å resolution of the crystal structure of the Escherichia coli medium chain length acyl-CoA thioesterase II. This enzyme is a close homolog of the human protein that interacts with the product of the HIV-1 Nef gene, sharing 45% amino acid sequence identity with it. The structure of the E. coli thioesterase II reveals a new tertiary fold, a ‘double hot dog’, showing an internal repeat with a basic unit that is structurally similar to the recently described β-hydroxydecanoyl thiol ester dehydrase. The catalytic site, inferred from the crystal structure and verified by site directed mutagenesis, involves novel chemistry and includes Asp 204, Gln 278 and Thr 228, which synergistically activate a nucleophilic water molecule.

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Figure 1: The molecular and crystal structure of TEII from E. coli.
Figure 2: The internal structural repeat in TEII and structural similarities with 4-hydroxybenzoyl-CoA thioesterase and β-hydroxydecanoyl thiol ester dehydrase.
Figure 3: The active site and catalytic mechanism of TEII.
Figure 4: Structure based sequence alignment of the TEII family members.

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Acknowledgements

We thank the EMBL outstation, Hamburg, for providing access to the synchrotron beamlines, and for outstanding assistance. A. Murzin (LMB, Cambridge, UK) was the first to note and point out to us the internal repeat in the structure of TEII. S. Garrard is gratefully acknowledged for conducting limited proteolysis on TEII. This study was funded by the National Institute of General Medical Sciences.

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Authors and Affiliations

  1. Department of Molecular Physiology and Biological Physics, University of Virginia, P.O. Box 800736, Charlottesville, 22908-0736, Virginia, USA

    Jia Li, Urszula Derewenda & Zygmunt S. Derewenda

  2. National Cancer Institute, Frederick and National Brookhaven Laboratory, Building 725A-X5, Upton, 11973, New York, USA

    Zbigniew Dauter

  3. Children's Hospital Oakland Research Institute, 747 Fifty-Second Street, Oakland, 94609, California, USA

    Stuart Smith

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  1. Jia Li
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  5. Zygmunt S. Derewenda
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Correspondence to Zygmunt S. Derewenda.

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Li, J., Derewenda, U., Dauter, Z. et al. Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme. Nat Struct Mol Biol 7, 555–559 (2000). https://doi.org/10.1038/76776

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