6n2y
From Proteopedia
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| - | ''' | + | {{Large structure}} |
| + | ==Bacillus PS3 ATP synthase class 1== | ||
| + | <StructureSection load='6n2y' size='340' side='right' caption='[[6n2y]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6n2y]] is a 22 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N2Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N2Y FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6n2d|6n2d]], [[6n2z|6n2z]], [[6n30|6n30]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></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=6n2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n2y OCA], [http://pdbe.org/6n2y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n2y RCSB], [http://www.ebi.ac.uk/pdbsum/6n2y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n2y ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | {{Large structure}} | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/A0A0M4TPJ7_BACP3 A0A0M4TPJ7_BACP3]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.[HAMAP-Rule:MF_00815][SAAS:SAAS00725627] [[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] [[http://www.uniprot.org/uniprot/A0A0M4U1P9_BACP3 A0A0M4U1P9_BACP3]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.[HAMAP-Rule:MF_01347] [[http://www.uniprot.org/uniprot/A0A0M3VGF9_BACP3 A0A0M3VGF9_BACP3]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[HAMAP-Rule:MF_01346] [[http://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] | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 6n2y" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Guo, H]] | [[Category: Guo, H]] | ||
| - | [[Category: Rubinstein, J | + | [[Category: Rubinstein, J L]] |
| + | [[Category: Bacterial atp synthase]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 06:54, 21 February 2019
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Bacillus PS3 ATP synthase class 1
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