Cryo-EM of ABC transporters: an ice-cold solution to everything?
- PMID: 33156959
- DOI: 10.1002/1873-3468.13989
Cryo-EM of ABC transporters: an ice-cold solution to everything?
Abstract
High-resolution cryo-EM has revolutionized how we look at ABC transporters and membrane proteins in general. An ever-increasing number of software tools and faster processing now allow dissecting the molecular details of nanomachines at atomic precision. Considering the further benefits of significantly reduced sample demands and increased speed, cryo-EM will dominate the structure determination of membrane proteins in the near future without compromising on data quality or detail. Moreover, improved and new algorithms make it now possible to resolve the conformational spectrum of macromolecular machines under turnover conditions and to analyze heterogeneous samples at high resolution. The future of cryo-EM is, therefore, bright, and the growing number of imaging facilities and groups active in this field will amplify this trend even further. Nevertheless, expectations have to be managed, as cryo-EM alone cannot provide an ultimate answer to all scientific questions. In this review, we discuss the capabilities and limitations of cryo-EM together with possible solutions for studies of ABC transporters.
Keywords: ABC transporters; conformational spectrum; cryo-EM; membrane proteins.
© 2020 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
Similar articles
-
Frozen motion: how cryo-EM changes the way we look at ABC transporters.Trends Biochem Sci. 2022 Feb;47(2):136-148. doi: 10.1016/j.tibs.2021.11.008. Epub 2021 Dec 17. Trends Biochem Sci. 2022. PMID: 34930672 Review.
-
Conformation space of a heterodimeric ABC exporter under turnover conditions.Nature. 2019 Jul;571(7766):580-583. doi: 10.1038/s41586-019-1391-0. Epub 2019 Jul 17. Nature. 2019. PMID: 31316210 Free PMC article.
-
Sample preparation of biological macromolecular assemblies for the determination of high-resolution structures by cryo-electron microscopy.Microscopy (Oxf). 2016 Feb;65(1):23-34. doi: 10.1093/jmicro/dfv367. Epub 2015 Dec 15. Microscopy (Oxf). 2016. PMID: 26671943 Review.
-
Cryo-electron Microscopy Structure and Transport Mechanism of a Wall Teichoic Acid ABC Transporter.mBio. 2020 Mar 17;11(2):e02749-19. doi: 10.1128/mBio.02749-19. mBio. 2020. PMID: 32184247 Free PMC article.
-
Structure of an endogenous mycobacterial MCE lipid transporter.Nature. 2023 Aug;620(7973):445-452. doi: 10.1038/s41586-023-06366-0. Epub 2023 Jul 26. Nature. 2023. PMID: 37495693
Cited by
-
Meta-Analysis of the Expansion in the Field of Structural Biology of ABC Transporters.Biodes Res. 2022 Sep 8;2022:9806979. doi: 10.34133/2022/9806979. eCollection 2022. Biodes Res. 2022. PMID: 37850125 Free PMC article. Review.
-
Nucleotide binding is the critical regulator of ABCG2 conformational transitions.Elife. 2023 Feb 10;12:e83976. doi: 10.7554/eLife.83976. Elife. 2023. PMID: 36763413 Free PMC article.
-
Plant Secondary Metabolite Transporters: Diversity, Functionality, and Their Modulation.Front Plant Sci. 2021 Oct 27;12:758202. doi: 10.3389/fpls.2021.758202. eCollection 2021. Front Plant Sci. 2021. PMID: 34777438 Free PMC article. Review.
-
Pharmacoproteomics of Brain Barrier Transporters and Substrate Design for the Brain Targeted Drug Delivery.Pharm Res. 2022 Jul;39(7):1363-1392. doi: 10.1007/s11095-022-03193-2. Epub 2022 Mar 7. Pharm Res. 2022. PMID: 35257288 Free PMC article. Review.
-
The Evolution of ABC Importers.J Mol Biol. 2025 Jun 1;437(11):169082. doi: 10.1016/j.jmb.2025.169082. Epub 2025 Mar 13. J Mol Biol. 2025. PMID: 40089147 Review.
References
-
- Kühlbrandt W (2014) The resolution revolution. Science 343, 1443-1444. http://dx.doi.org/10.1126/science.1251652
-
- Liao M, Cao E, Julius D and Cheng Y (2013) Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107-112. http://dx.doi.org/10.1038/nature12822
-
- Cao E, Liao M, Cheng Y and Julius D (2013) TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 504, 113-118. http://dx.doi.org/10.1038/nature12823
-
- Kim JM, Wu S, Tomasiak TM, Mergel C, Winter MB, Stiller SB, Robles-Colmanares Y, Stroud RM, Tampé R, Craik CS et al. (2015) Subnanometre-resolution electron cryomicroscopy structure of a heterodimeric ABC exporter. Nature 517, 396-400. http://dx.doi.org/10.1038/nature13872
-
- Oldham ML, Grigorieff N and Chen J (2016) Structure of the transporter associated with antigen processing trapped by herpes simplex virus. Elife 5, e21829. http://dx.doi.org/10.7554/elife.21829
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources