6LUL

NMR structure and dynamics studies of yeast respiratory super-complex factor 2 in micelles

Summary for 6LUL

• Entry DOI: 10.2210/pdb6lul/pdb
• NMR Information: BMRB: 36312
• Descriptor: Respiratory supercomplex factor 2, mitochondrial (1 entity in total)
• Functional Keywords: membrane protein, respiratory supercomplex factor, structural protein
• Biological source: Saccharomyces cerevisiae S288C (Baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 54520.34

Authors

Zhou, S.,Pontus, P.,Peter, B.,Maler, L.,Adelroth, P. (deposition date: 2020-01-29, release date: 2020-10-07, Last modification date: 2024-05-01)

Primary citation

Zhou, S.,Pettersson, P.,Huang, J.,Brzezinski, P.,Pomes, R.,Maler, L.,Adelroth, P.
NMR Structure and Dynamics Studies of Yeast Respiratory Supercomplex Factor 2.
Structure, 29:275-, 2021

PubMed Abstract: The 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 bc 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 α helices and five putative transmembrane (TM) α 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.

PubMed: 32905793
DOI: 10.1016/j.str.2020.08.008

Experimental method

SOLUTION NMR