The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
De novo design of a transmembrane Zn 2+ -transporting four-helix bundle
Open accessAbstract
The design of functional membrane proteins from first principles represents a grand challenge in chemistry and structural biology. Here, we report the design of a membrane-spanning, four-helical bundle that transports first-row transition metal ions Zn 2+ and Co 2+ , but not Ca 2+ , across membranes. The conduction path was designed to contain two di-metal binding sites that bind with negative cooperativity. X-ray crystallography and solid-state and solution nuclear magnetic resonance indicate that the overall helical bundle is formed from two tightly interacting pairs of helices, which form individual domains that interact weakly along a more dynamic interface. Vesicle flux experiments show that as Zn 2+ ions diffuse down their concentration gradients, protons are antiported. These experiments illustrate the feasibility of designing membrane proteins with predefined structural and dynamic properties.
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Metadata
- Authors
- Joh, N. H., Wang, T., Bhate, M. P., Acharya, R., Wu, Y., Grabe, M., Hong, M., Grigoryan, G., & DeGrado, W. F.
- Venue
- Science
- Published
- 2014-12-19
- Volume
- 346
- Issue
- 6216
- Pages
- 1520-1524
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1974312616
- Cited by
- 298
- References
- 59
- FWCI
- 11.56
- Type
- journal article
- Language
- en
- Open access
- green
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