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The 3.5 Å CryoEM Structure of Nanodisc Reconstituted Yeast Vacuolar ATPase V(o) Proton Channel
The molecular mechanism of transmembrane proton translocation in rotary motor ATPases is not fully understood. Here we report the 3.5 Å resolution cryoEM structure of the lipid nanodisc-reconstituted V(o) proton channel of the yeast vacuolar H(+)-ATPase, captured in a physiologically relevant, autoi...
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| Vydáno v: | Mol Cell |
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| Hlavní autoři: | , , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2018
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5893162/ https://ncbi.nlm.nih.gov/pubmed/29526695 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.molcel.2018.02.006 |
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