F-ATPase

<h2 id="structure">Structure</h2>
<p class="note">See also: <a href="/facts/ATP_synthase/5NBMxsVX">ATP synthase § Structure and function</a></p>
<p>Fo-F1 particles are mainly formed of <a href="/facts/Polypeptides/C4ltc7UG">polypeptides</a>. The F1-particle contains 5 types of polypeptides, with the composition-ratio—3α:3β:1δ:1γ:1ε. The Fo has the 1a:2b:12c composition. Together they form a rotary motor. As the protons bind to the subunits of the Fo domains, they cause parts of it to rotate. This rotation is propagated by a 'camshaft' to the F1 domain. ADP and Pi (inorganic phosphate) bind spontaneously to the three β subunits of the F1 domain, so that every time it goes through a 120° rotation ATP is released (rotational catalysis).
</p><p>The Fo domains sits within the membrane, spanning the phospholipid bilayer, while the F1 domain extends into the cytosol of the cell to facilitate the use of newly synthesized ATP.
</p><p>The Bovine Mitochondrial F1-ATPase Complexed with the <a href="/facts/Inhibitor_protein/o9QF2LKh">inhibitor protein</a> If1 is commonly cited in the relevant literature. Examples of its use may be found in many cellular fundamental metabolic activities such as <a href="/facts/Acidosis/hmfAo1uR">acidosis</a> and <a href="/facts/Alkalosis/SoUSH8No">alkalosis</a> and respiratory gas exchange.
</p><p>The o in the Fo stands for <a href="/facts/Oligomycin/FbV6fUav">oligomycin</a>, because oligomycin is able to inhibit its function.
</p>
<h2 id="n-atpase">N-ATPase</h2>
<p>N-ATPases are a group of F-type ATPases without a <a href="/facts/ATP_synthase_delta%2fOSCP_subunit/LlIqLI6F">delta/OSCP subunit</a>, found in bacteria and a group of archaea via horizontal gene transfer. They transport sodium ions instead of protons and tend to hydrolyze ATP. They form a distinct group that is further apart from usual F-ATPases than A-ATPases are from V-ATPases.<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a>
</p>

<h2 id="references">References</h2>

<ol>
<li id="fn:1"><p>Lodish H (2008). Molecular Cell Biology (Kindle ed.). W. H. Freeman. p. 553. <a href="https://archive.org/details/molecularcellbio00harv_624" target="_blank">https://archive.org/details/molecularcellbio00harv_624</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li>
<li id="fn:2"><p>Lodish H (2008). Molecular Cell Biology (Kindle ed.). W. H. Freeman. p. 553. <a href="https://archive.org/details/molecularcellbio00harv_624" target="_blank">https://archive.org/details/molecularcellbio00harv_624</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li>
<li id="fn:3"><p>Ren Q, Paulsen IT (2009). "Transport, Solute". Encyclopedia of Microbiology (Third ed.). Academic Press. pp. 529–544. doi:10.1016/B978-012373944-5.00107-3. ISBN 978-0-12-373944-5. <a href="978-0-12-373944-5" target="_blank">978-0-12-373944-5</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li>
<li id="fn:4"><p>Dibrova, DV; Galperin, MY; Mulkidjanian, AY (15 June 2010). "Characterization of the N-ATPase, a distinct, laterally transferred Na+-translocating form of the bacterial F-type membrane ATPase". Bioinformatics. 26 (12): 1473–6. doi:10.1093/bioinformatics/btq234. PMC 2881411. PMID 20472544. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2881411" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2881411</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li>
</ol>

F-ATPase open-in-new

F-ATPase