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Structural and molecular mechanisms for membrane protein biogenesis by the Oxa1 superfamily

Nature Structural & Molecular Biology volume 28, pages 234–239 (2021)Cite this article

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Abstract

Members of the Oxa1 superfamily perform membrane protein insertion in bacteria, the eukaryotic endoplasmic reticulum (ER), and endosymbiotic organelles. Here, we review recent structures of the three ER-resident insertases and discuss the extent to which structure and function are conserved with their bacterial counterpart YidC.

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Fig. 1: The Oxa1 superfamily.
Fig. 2: Members of the Oxa1 superfamily share a common membrane domain fold.
Fig. 3: Oxa1 homologs utilize cytoplasmically exposed coiled-coils for substrate recruitment.

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Acknowledgements

This work was supported by an EMBO Long Term Fellowship (ALTF 1230-2013) to M.A.M. and by the DFG through the Leibniz Programme (SI 586/6-1) and TRR83 (TP22) to I.S.

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  1. These authors contributed equally: Melanie A. McDowell, Michael Heimes.

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  1. Heidelberg University Biochemistry Center (BZH), Heidelberg, Germany

    Melanie A. McDowell, Michael Heimes & Irmgard Sinning

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M.A.M., M.H. and I.S. wrote the manuscript.

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McDowell, M.A., Heimes, M. & Sinning, I. Structural and molecular mechanisms for membrane protein biogenesis by the Oxa1 superfamily. Nat Struct Mol Biol 28, 234–239 (2021). https://doi.org/10.1038/s41594-021-00567-9

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