View source for 5fik


==Bovine mitochondrial ATP synthase state 3a==
<SX load='5fik' size='340' side='right' viewer='molstar' caption='[[5fik]], [[Resolution|resolution]] 6.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fik]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FIK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FIK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fik OCA], [https://pdbe.org/5fik PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fik RCSB], [https://www.ebi.ac.uk/pdbsum/5fik PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fik ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATPA_BOVIN ATPA_BOVIN] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Adenosine triphosphate (ATP), the chemical energy currency of biology, is synthesized in eukaryotic cells primarily by the mitochondrial ATP synthase. ATP synthases operate by a rotary catalytic mechanism where proton translocation through the membrane-inserted F0 region is coupled to ATP synthesis in the catalytic F1 region via rotation of a central rotor subcomplex. We report here single particle electron cryomicroscopy (cryo-EM) analysis of the bovine mitochondrial ATP synthase. Combining cryo-EM data with bioinformatic analysis allowed us to determine the fold of the a subunit, suggesting a proton translocation path through the F0 region that involves both the a and b subunits. 3D classification of images revealed seven distinct states of the enzyme that show different modes of bending and twisting in the intact ATP synthase. Rotational fluctuations of the c8-ring within the F0 region support a Brownian ratchet mechanism for proton-translocation driven rotation in ATP synthases.

Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.,Zhou A, Rohou A, Schep DG, Bason JV, Montgomery MG, Walker JE, Grigorieff N, Rubinstein JL Elife. 2015 Oct 6;4. doi: 10.7554/eLife.10180. PMID:26439008<ref>PMID:26439008</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5fik" style="background-color:#fffaf0;"></div>

==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Bason JV]]
[[Category: Grigorieff N]]
[[Category: Montgomery MG]]
[[Category: Rohou A]]
[[Category: Rubinstein JL]]
[[Category: Schep DG]]
[[Category: Walker JE]]
[[Category: Zhou A]]