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Crystal structure of the human sterol transporter ABCG5/ABCG8
Open accessAbstract
ATP binding cassette (ABC) transporters play critical roles in maintaining sterol balance in higher eukaryotes. The ABCG5/ABCG8 heterodimer (G5G8) mediates excretion of neutral sterols in liver and intestines. Mutations disrupting G5G8 cause sitosterolaemia, a disorder characterized by sterol accumulation and premature atherosclerosis. Here we use crystallization in lipid bilayers to determine the X-ray structure of human G5G8 in a nucleotide-free state at 3.9 Å resolution, generating the first atomic model of an ABC sterol transporter. The structure reveals a new transmembrane fold that is present in a large and functionally diverse superfamily of ABC transporters. The transmembrane domains are coupled to the nucleotide-binding sites by networks of interactions that differ between the active and inactive ATPases, reflecting the catalytic asymmetry of the transporter. The G5G8 structure provides a mechanistic framework for understanding sterol transport and the disruptive effects of mutations causing sitosterolaemia.
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Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353
The Amber biomolecular simulation programs
Case, D. A., Cheatham, T. E., Darden, T., Gohlke, H., Luo, R., Merz, K. M., Onufriev, A., Simmerling, C., Wang, B., & Woods, R. J. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20290 · Cited by 9,535
Large-scale determination of previously unsolved protein structures using evolutionary information
Ovchinnikov, S., Kinch, L., Park, H., Liao, Y., Pei, J., Kim, D. E., Kamisetty, H., Grishin, N. V., & Baker, D. (2015) · eLife · doi:10.7554/elife.09248 · Cited by 222
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Cryo-EM structures of a human ABCG2 mutant trapped in ATP-bound and substrate-bound states
Manolaridis, I., Jackson, S. M., Taylor, N. M. I., Kowal, J., Stahlberg, H., & Locher, K. P. (2018) · Nature · doi:10.1038/s41586-018-0680-3 · Cited by 228
Ins and outs of AlphaFold2 transmembrane protein structure predictions
Hegedűs, T., Geisler, M., Lukács, G. L., & Farkas, B. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-04112-1 · Cited by 127
Comparison of mechanistic transport cycle models of ABC exporters
Szöllősi, D., Rose-Sperling, D., Hellmich, U. A., & Stockner, T. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.10.028 · Cited by 107
Metadata
- Authors
- Lee, J.-Y., Kinch, L. N., Borek, D. M., Wang, J., Wang, J., Urbatsch, I. L., Xie, X.-S., Grishin, N. V., Cohen, J. C., Otwinowski, Z., Hobbs, H. H., & Rosenbaum, D. M.
- Venue
- Nature
- Published
- 2016-05-04
- Volume
- 533
- Issue
- 7604
- Pages
- 561-564
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2346768082
- Cited by
- 269
- References
- 3
- FWCI
- 18.08
- Type
- journal article
- Language
- en
- Open access
- green
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- Lee, J.-Y., Kinch, L. N., Borek, D. M., Wang, J., Wang, J., Urbatsch, I. L., Xie, X.-S., Grishin, N. V., Cohen, J. C., Otwinowski, Z., Hobbs, H. H., & Rosenbaum, D. M. (2016). Crystal structure of the human sterol transporter ABCG5/ABCG8. Nature. https://doi.org/10.1038/nature17666
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