+ Site Statistics
References:
54,258,434
Abstracts:
29,560,870
PMIDs:
28,072,757
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases



Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases



Molecules 24(3)



F-ATP synthases use proton flow through the FO domain to synthesize ATP in the F₁ domain. In Escherichia coli, the enzyme consists of rotor subunits γεc10 and stator subunits (αβ)₃δab₂. Subunits c10 or (αβ)₃ alone are rotationally symmetric. However, symmetry is broken by the b₂ homodimer, which together with subunit δa, forms a single eccentric stalk connecting the membrane embedded FO domain with the soluble F₁ domain, and the central rotating and curved stalk composed of subunit γε. Although each of the three catalytic binding sites in (αβ)₃ catalyzes the same set of partial reactions in the time average, they might not be fully equivalent at any moment, because the structural symmetry is broken by contact with b₂δ in F₁ and with ba in FO. We monitored the enzyme's rotary progression during ATP hydrolysis by three single-molecule techniques: fluorescence video-microscopy with attached actin filaments, Förster resonance energy transfer between pairs of fluorescence probes, and a polarization assay using gold nanorods. We found that one dwell in the three-stepped rotary progression lasting longer than the other two by a factor of up to 1.6. This effect of the structural asymmetry is small due to the internal elastic coupling.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 066446270

Download citation: RISBibTeXText

PMID: 30704145

DOI: 10.3390/molecules24030504


Related references

Mechanisms of rotary Atp synthases revealed by single-molecule rotation studies. Biochimica et Biophysica Acta (Bba) - Bioenergetics 1857: e13, 2016

Single-molecule fluorescence resonance energy transfer techniques on rotary ATP synthases. Biological Chemistry 392(1-2): 135-142, 2011

Coupling H+ transport to rotary catalysis in F-type ATP synthases: structure and organization of the transmembrane rotary motor. The Journal of Experimental Biology 203(1): 17, 2000

Coupling H(+) transport to rotary catalysis in F-type ATP synthases: structure and organization of the transmembrane rotary motor. Journal of Experimental Biology 203(Pt 1): 9-17, 1999

Elastic deformations of the rotary double motor of single F(o)F(1)-ATP synthases detected in real time by Förster resonance energy transfer. Biochimica et Biophysica Acta 1817(10): 1722-1731, 2013

Elastic deformations of the rotary double motor of single FOF1-ATP synthases detected in real time by Forster resonance energy transfer. 2012

Three-color Förster resonance energy transfer within single F₀F₁-ATP synthases: monitoring elastic deformations of the rotary double motor in real time. Journal of Biomedical Optics 17(1): 011004, 2012

Structural transitions in transcription initiation Kinetic and single-molecule kinetic analyses. Biophysical Journal 80(1 Part 2): 3a, 2001

The Structural Enzymology of Iterative Aromatic Polyketide Synthases: A Critical Comparison with Fatty Acid Synthases. Annual Review of Biochemistry 87: 503-531, 2018

Using a Single Set of Structural and Kinetic Parameters of the Microheterogeneous Model to Describe the Sorption and Kinetic Properties of Ion-Exchange Membranes. Petroleum Chemistry 58(6): 465-473, 2018

Both GA2, GM2, and GD2 synthases and GM1b, GD1a, and GT1b synthases are single enzymes in Golgi vesicles from rat liver. Proceedings of the National Academy of Sciences of the United States of America 85(19): 7044-7048, 1988

The rotary binding change mechanism of ATP synthases. Biochimica et Biophysica Acta 1458(2-3): 270-275, 2000

Guest-induced asymmetry in a metal-organic porous solid with reversible single-crystal-to-single-crystal structural transformation. Journal of the American Chemical Society 127(49): 17152-3, 2005

Functional asymmetry of the F(0) motor in bacterial ATP synthases. Molecular Microbiology 72(2): 479-490, 2009

Quaternary structure of ATP synthases: Symmetry and asymmetry in the F-1 moiety. Journal of Bioenergetics and Biomembranes 24(5): 429-433, 1992