6lul
From Proteopedia
NMR structure and dynamics studies of yeast respiratory super-complex factor 2 in micelles
Structural highlights
Function[RCF2_YEAST] Assembly factor that plays a role in the assembly of the respiratory chain supercomplexes (SCs) composed of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV). May be required for late-stage assembly of the COX12 and COX13 subunits (PubMed:22342701, PubMed:22310663). Required for the generation and maintenance of a normal proton motive force (PMF) across the inner mitochondrial membrane (IMM) by preventing proton leakage through an inactive population of CIV that accumulates when RCF1 and/or RCF2 proteins are absent (PubMed:30683696, PubMed:31591265).[1] [2] [3] [4] Publication Abstract from PubMedThe Saccharomyces cerevisiae respiratory supercomplex factor 2 (Rcf2) is a 224-residue protein located in the mitochondrial inner membrane where it is involved in the formation of supercomplexes composed of cytochrome bc1 and cytochrome c oxidase. We previously demonstrated that Rcf2 forms a dimer in dodecylphosphocholine micelles, and here we report the solution NMR structure of this Rcf2 dimer. Each Rcf2 monomer has two soluble alpha helices and five putative transmembrane (TM) alpha helices, including an unexpectedly charged TM helix at the C terminus, which mediates dimer formation. The NOE contacts indicate the presence of inter-monomer salt bridges and hydrogen bonds at the dimer interface, which stabilize the Rcf2 dimer structure. Moreover, NMR chemical shift change mapping upon lipid titrations as well as molecular dynamics analysis reveal possible structural changes upon embedding Rcf2 into a native lipid environment. Our results contribute to the understanding of respiratory supercomplex formation and regulation. NMR Structure and Dynamics Studies of Yeast Respiratory Supercomplex Factor 2.,Zhou S, Pettersson P, Huang J, Brzezinski P, Pomes R, Maler L, Adelroth P Structure. 2020 Sep 3. pii: S0969-2126(20)30290-2. doi:, 10.1016/j.str.2020.08.008. PMID:32905793[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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