View source for 6n30


==Bacillus PS3 ATP synthase class 3==
<SX load='6n30' size='340' side='right' viewer='molstar' caption='[[6n30]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6n30]] is a 22 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=6N30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N30 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]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=6n30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n30 OCA], [https://pdbe.org/6n30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n30 RCSB], [https://www.ebi.ac.uk/pdbsum/6n30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n30 ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/A0A0M5MQR7_BACP3 A0A0M5MQR7_BACP3] Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530][SAAS:SAAS00872986]
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== 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>
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<div class="pdbe-citations 6n30" style="background-color:#fffaf0;"></div>

==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
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[[Category: Bacillus sp. PS3]]
[[Category: Large Structures]]
[[Category: Guo H]]
[[Category: Rubinstein JL]]