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{{Large structure}}
 
==Bacillus PS3 ATP synthase membrane region==
==Bacillus PS3 ATP synthase membrane region==
<StructureSection load='6n2d' size='340' side='right' caption='[[6n2d]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<SX load='6n2d' size='340' side='right' viewer='molstar' caption='[[6n2d]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6n2d]] is a 13 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N2D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N2D FirstGlance]. <br>
<table><tr><td colspan='2'>[[6n2d]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._PS3 Bacillus sp. PS3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N2D FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6n2y|6n2y]], [[6n2z|6n2z]], [[6n30|6n30]]</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]] 3.3&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6n2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n2d OCA], [http://pdbe.org/6n2d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n2d RCSB], [http://www.ebi.ac.uk/pdbsum/6n2d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n2d ProSAT]</span></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=6n2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n2d OCA], [https://pdbe.org/6n2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n2d RCSB], [https://www.ebi.ac.uk/pdbsum/6n2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n2d ProSAT]</span></td></tr>
</table>
</table>
{{Large structure}}
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ATPL_BACP3 ATPL_BACP3]] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.[HAMAP-Rule:MF_01396]  Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396]  
[https://www.uniprot.org/uniprot/ATPL_BACP3 ATPL_BACP3] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.[HAMAP-Rule:MF_01396]  Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
ATP synthases produce ATP from ADP and inorganic phosphate with energy from a transmembrane proton motive force. Bacterial ATP synthases have been studied extensively because they are the simplest form of the enzyme and because of the relative ease of genetic manipulation of these complexes. We expressed the Bacillus PS3 ATP synthase in Eschericia coli, purified it, and imaged it by cryo-EM, allowing us to build atomic models of the complex in three rotational states. The position of subunit epsilon shows how it is able to inhibit ATP hydrolysis while allowing ATP synthesis. The architecture of the membrane region shows how the simple bacterial ATP synthase is able to perform the same core functions as the equivalent, but more complicated, mitochondrial complex. The structures reveal the path of transmembrane proton translocation and provide a model for understanding decades of biochemical analysis interrogating the roles of specific residues in the enzyme.
 
Structure of a bacterial ATP synthase.,Guo H, Suzuki T, Rubinstein JL Elife. 2019 Feb 6;8. pii: 43128. doi: 10.7554/eLife.43128. PMID:30724163<ref>PMID:30724163</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==See Also==
</div>
*[[ATPase 3D structures|ATPase 3D structures]]
<div class="pdbe-citations 6n2d" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Guo, H]]
[[Category: Bacillus sp. PS3]]
[[Category: Rubinstein, J L]]
[[Category: Large Structures]]
[[Category: Hydrolase]]
[[Category: Guo H]]
[[Category: Rubinstein JL]]
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