Cargando…
Binding of the Inhibitor Protein IF(1) to Bovine F(1)-ATPase
In the structure of bovine F(1)-ATPase inhibited with residues 1–60 of the bovine inhibitor protein IF(1), the α-helical inhibitor interacts with five of the nine subunits of F(1)-ATPase. In order to understand the contributions of individual amino acid residues to this complex binding mode, N-termi...
Autores principales: | Bason, John V., Runswick, Michael J., Fearnley, Ian M., Walker, John E. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3041923/ https://www.ncbi.nlm.nih.gov/pubmed/21192948 http://dx.doi.org/10.1016/j.jmb.2010.12.025 |
Ejemplares similares
-
The structure of F(1)-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF(1)
por: Robinson, Graham C., et al.
Publicado: (2013) -
The affinity purification and characterization of ATP synthase complexes from mitochondria
por: Runswick, Michael J., et al.
Publicado: (2013) -
How release of phosphate from mammalian F(1)-ATPase generates a rotary substep
por: Bason, John V., et al.
Publicado: (2015) -
Organization of Subunits in the Membrane Domain of the Bovine F-ATPase Revealed by Covalent Cross-linking
por: Lee, Jennifer, et al.
Publicado: (2015) -
Purification, characterization and crystallization of the F-ATPase from Paracoccus denitrificans
por: Morales-Rios, Edgar, et al.
Publicado: (2015)