Cargando…
Structure of Escherichia coli respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation
Respiratory complex I is a multi-subunit membrane protein complex that reversibly couples NADH oxidation and ubiquinone reduction with proton translocation against transmembrane potential. Complex I from Escherichia coli is among the best functionally characterized complexes, but its structure remai...
Autores principales: | Kolata, Piotr, Efremov, Rouslan G |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8357420/ https://www.ncbi.nlm.nih.gov/pubmed/34308841 http://dx.doi.org/10.7554/eLife.68710 |
Ejemplares similares
-
Structure of SARS-CoV-2 M protein in lipid nanodiscs
por: Dolan, Kimberly A, et al.
Publicado: (2022) -
Cryo-EM structure of the potassium-chloride cotransporter KCC4 in lipid nanodiscs
por: Reid, Michelle S, et al.
Publicado: (2020) -
Sterol derivative binding to the orthosteric site causes conformational changes in an invertebrate Cys-loop receptor
por: De Gieter, Steven, et al.
Publicado: (2023) -
Structure and dynamics of a nanodisc by integrating NMR, SAXS and SANS experiments with molecular dynamics simulations
por: Bengtsen, Tone, et al.
Publicado: (2020) -
A mutation uncouples the tubulin conformational and GTPase cycles, revealing allosteric control of microtubule dynamics
por: Geyer, Elisabeth A, et al.
Publicado: (2015)