ATP synthase fromhas an elaborated canonical F-domain and conventional catalytic sites.

TitleATP synthase fromhas an elaborated canonical F-domain and conventional catalytic sites.
Publication TypeJournal Article
Year of Publication2018
AuthorsMontgomery, MG, Gahura, O, Leslie, AGW, Zíková, A, Walker, JE
JournalProc Natl Acad Sci U S A
Volume115
Issue9
Pagination2102-2107
Date Published2018 Feb 27
ISSN1091-6490
Abstract

The structures and functions of the components of ATP synthases, especially those subunits involved directly in the catalytic formation of ATP, are widely conserved in metazoans, fungi, eubacteria, and plant chloroplasts. On the basis of a map at 32.5-Å resolution determined in situ in the mitochondria ofby electron cryotomography, it has been proposed that the ATP synthase in this species has a noncanonical structure and different catalytic sites in which the catalytically essential arginine finger is provided not by the α-subunit adjacent to the catalytic nucleotide-binding site as in all species investigated to date, but rather by a protein, p18, found only in the euglenozoa. A crystal structure at 3.2-Å resolution of the catalytic domain of the same enzyme demonstrates that this proposal is incorrect. In many respects, the structure is similar to the structures of F-ATPases determined previously. The αβ-spherical portion of the catalytic domain in which the three catalytic sites are found, plus the central stalk, are highly conserved, and the arginine finger is provided conventionally by the α-subunits adjacent to each of the three catalytic sites found in the β-subunits. Thus, the enzyme has a conventional catalytic mechanism. The structure differs from previous described structures by the presence of a p18 subunit, identified only in the euglenozoa, associated with the external surface of each of the three α-subunits, thereby elaborating the F-domain. Subunit p18 is a pentatricopeptide repeat (PPR) protein with three PPRs and appears to have no function in the catalytic mechanism of the enzyme.

DOI10.1073/pnas.1720940115
Alternate JournalProc. Natl. Acad. Sci. U.S.A.
Citation Key10.1073/pnas.1720940115
PubMed ID29440423