Solution structure of subunit F(6) from the peripheral stalk region of ATP synthase from bovine heart mitochondria.

TitleSolution structure of subunit F(6) from the peripheral stalk region of ATP synthase from bovine heart mitochondria.
Publication TypeJournal Article
Year of Publication2004
AuthorsCarbajo, RJ, Silvester, JA, Runswick, MJ, Walker, JE, Neuhaus, D
JournalJ Mol Biol
Volume342
Issue2
Pagination593-603
Date Published2004 Sep 10
ISSN0022-2836
KeywordsAnimals, Cattle, Magnetic Resonance Spectroscopy, Mitochondria, Mitochondrial Proton-Translocating ATPases, Myocardium, Protein Structure, Tertiary
Abstract

The ATP synthase enzyme structure includes two stalk assemblies, the central stalk and the peripheral stalk. Catalysis involves rotation of the central stalk assembly together with the membrane-embedded ring of c-subunits driven by the trans-membrane proton-motive force, while the alpha and beta-subunits of F(1) are prevented from co-rotating by their attachment to the peripheral stalk. In the absence of structures of either the intact peripheral stalk or larger complexes containing it, we are studying its individual components and their interactions to build up an overall picture of its structure. Here, we describe an NMR structural characterisation of F(6), which is a 76-residue protein located in the peripheral stalk of the bovine ATP synthase and is essential for coupling between the proton-motive force and catalysis. Isolated F(6) has a highly flexible structure comprising two helices packed together through a loose hydrophobic core and connected by an unstructured linker. Analysis of chemical shifts, (15)N relaxation and RDC measurements confirm that the F(6) structure is flexible on a wide range of timescales ranging from nanoseconds to seconds. The relationship between this structure for isolated F(6) and its role in the intact peripheral stalk is discussed.

DOI10.1016/j.jmb.2004.07.013
Alternate JournalJ. Mol. Biol.
Citation Key10.1016/j.jmb.2004.07.013
PubMed ID15327958