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Three-dimensional structure of a bacterial oxalate transporter

Nature Structural Biology volume 9, pages 597–600 (2002)Cite this article

Abstract

The major facilitator superfamily (MFS) represents one of the largest classes of evolutionarily related membrane transporter proteins. Here we present the three-dimensional structure at 6.5 Å resolution of a bacterial member of this superfamily, OxlT. The structure, derived from an electron crystallographic analysis of two-dimensional crystals, reveals that the 12 helices in the OxlT molecule are arranged around a central cavity, which is widest at the center of the membrane. The helices divide naturally into three groups: a peripheral set comprising helices 3, 6, 9 and 12; a second set comprising helices 2, 5, 8 and 11 that faces the central substrate transport pathway across most of the length of the membrane; and a third set comprising helices 1, 4, 7 and 10 that participate in the pathway either on the cytoplasmic side (4 and 10) or on the periplasmic side (1 and 7). Overall, the architecture of the protein is remarkably symmetric, providing a compelling molecular explanation for the ability of such transporters to carry out bi-directional substrate transport.

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Figure 1: Fitted lattice lines for three selected reflections showing the quality of the fit for phases (upper panels) and amplitudes (lower panels) along the z* axis.
Figure 2: Stereo view of the three-dimensional density map of OxlT, contoured at 1.3 σ.
Figure 3: Horizontal sections (3 Å thick) from the density map at intervals of 7.5 Å from the center.
Figure 4: Schematic analysis of structure.

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Acknowledgements

We thank L. Ye for generous assistance with purification of OxIT and D. Bliss for assistance with preparation of figures. This work was supported by grants to S.S. from the intramural program at the National Institutes of Health and to P.C.M. from the National Science Foundation.

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Author notes

  1. Teruhisa Hirai, Jürgen A.W. Heymann, Dan Shi, Rafiquel Sarker and Peter C. Maloney: These authors contributed equally to this work.

Authors and Affiliations

  1. Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, 20892, Maryland, USA

    Teruhisa Hirai, Jürgen A.W. Heymann, Dan Shi & Sriram Subramaniam

  2. Department of Physiology, The Johns Hopkins University School of Medicine, Baltimore, 21205, Maryland, USA

    Rafiquel Sarker & Peter C. Maloney

Authors
  1. Teruhisa Hirai
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Correspondence to Sriram Subramaniam.

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Hirai, T., Heymann, J., Shi, D. et al. Three-dimensional structure of a bacterial oxalate transporter. Nat Struct Mol Biol 9, 597–600 (2002). https://doi.org/10.1038/nsb821

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