Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase

Mark E. Girvin, Vinit K. Rastogi, Frits Abildgaard, John L. Markley, Robert H. Fillingame

Research output: Contribution to journalArticle

252 Citations (Scopus)

Abstract

Subunit c is the H+-translocating component of the F1F0 ATP synthase complex. H+ transport is coupled to conformational changes that ultimately lead to ATP synthesis by the enzyme. The properties of the monomeric subunit in a single-phase solution of chloroform-methanol-water (4:4:1) have been shown to mimic those of the protein in the native complex. Triple resonance NMR experiments were used to determine the complete structure of monomeric subunit c in this solvent mixture. The structure of the protein was defined by >2000 interproton distances, 64 3(Nα), and 43 hydrogen-bonding NMR- derived restraints. The root mean squared deviation for the backbone atoms of the two transmembrane helices was 0.63 Å. The protein folds as a hairpin of two antiparallel helical segments, connected by a short structured loop. The conserved Arg41-Gln42-Pro43 form the top of this loop. The essential H+- transporting Asp61 residue is located at a slight break in the middle of the C-terminal helix, just prior to Pro64. The C-terminal helix changes direction by 30 ± 5°at the conserved Pro64. In its protonated form, the Asp61 lies in a cavity created by the absence of side chains at Gly23 and Gly27 in the N- terminal helix. The shape and charge distribution of the molecular surface of the monomeric protein suggest a packing arrangement for the oligomeric protein in the F(o) complex, with the front face of one monomer packing favorably against the back face of a second monomer. The packing suggests that the proton (cation) binding site lies between packed pairs of adjacent subunit c.

Original languageEnglish (US)
Pages (from-to)8817-8824
Number of pages8
JournalBiochemistry
Volume37
Issue number25
DOIs
StatePublished - Jun 23 1998

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Proteins
Monomers
Nuclear magnetic resonance
Hydrogen Bonding
Chloroform
Charge distribution
Methanol
Cations
Protons
Membrane Proteins
Adenosine Triphosphate
Binding Sites
Hydrogen bonds
F1F0-ATP synthase
Water
Enzymes
Atoms
Experiments
Direction compound

ASJC Scopus subject areas

  • Biochemistry

Cite this

Girvin, M. E., Rastogi, V. K., Abildgaard, F., Markley, J. L., & Fillingame, R. H. (1998). Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase. Biochemistry, 37(25), 8817-8824. https://doi.org/10.1021/bi980511m

Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase. / Girvin, Mark E.; Rastogi, Vinit K.; Abildgaard, Frits; Markley, John L.; Fillingame, Robert H.

In: Biochemistry, Vol. 37, No. 25, 23.06.1998, p. 8817-8824.

Research output: Contribution to journalArticle

Girvin, ME, Rastogi, VK, Abildgaard, F, Markley, JL & Fillingame, RH 1998, 'Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase', Biochemistry, vol. 37, no. 25, pp. 8817-8824. https://doi.org/10.1021/bi980511m
Girvin ME, Rastogi VK, Abildgaard F, Markley JL, Fillingame RH. Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase. Biochemistry. 1998 Jun 23;37(25):8817-8824. https://doi.org/10.1021/bi980511m
Girvin, Mark E. ; Rastogi, Vinit K. ; Abildgaard, Frits ; Markley, John L. ; Fillingame, Robert H. / Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase. In: Biochemistry. 1998 ; Vol. 37, No. 25. pp. 8817-8824.
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