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5ara

From Proteopedia

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Current revision

Bovine mitochondrial ATP synthase state 1a

5ara, resolution 6.70Å

Structural highlights

5ara is a 21 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 6.7Å
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ara"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[5ara]] 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=5ARA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ARA FirstGlance]. <br>
-</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=5ara FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ara OCA], [https://pdbe.org/5ara PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ara RCSB], [https://www.ebi.ac.uk/pdbsum/5ara PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ara ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.7&#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=5ara FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ara OCA], [https://pdbe.org/5ara PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ara RCSB], [https://www.ebi.ac.uk/pdbsum/5ara PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ara ProSAT]</span></td></tr>
 </table>
 == Function ==

5ara

From Proteopedia

Current revision

Bovine mitochondrial ATP synthase state 1a

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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