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==Solution structure of subunit c of F1Fo-ATP synthase from the thermophilic bacillus PS3== | ==Solution structure of subunit c of F1Fo-ATP synthase from the thermophilic bacillus PS3== | ||
<StructureSection load='1wu0' size='340' side='right' caption='[[1wu0 | <StructureSection load='1wu0' size='340' side='right'caption='[[1wu0]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1wu0]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1wu0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._PS3 Bacillus sp. PS3]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WU0 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1wu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wu0 OCA], [https://pdbe.org/1wu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wu0 RCSB], [https://www.ebi.ac.uk/pdbsum/1wu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wu0 ProSAT]</span></td></tr> | |||
<tr | </table> | ||
== Function == | |||
<table> | [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] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wu/1wu0_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wu/1wu0_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wu0 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[ATPase|ATPase]] | *[[ATPase 3D structures|ATPase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus sp. | [[Category: Bacillus sp. PS3]] | ||
[[Category: Akutsu | [[Category: Large Structures]] | ||
[[Category: Ikegami | [[Category: Akutsu H]] | ||
[[Category: Nakano | [[Category: Ikegami T]] | ||
[[Category: Suzuki | [[Category: Nakano T]] | ||
[[Category: Yoshida | [[Category: Suzuki T]] | ||
[[Category: Yoshida M]] | |||
Latest revision as of 16:49, 9 May 2024
Solution structure of subunit c of F1Fo-ATP synthase from the thermophilic bacillus PS3Solution structure of subunit c of F1Fo-ATP synthase from the thermophilic bacillus PS3
Structural highlights
FunctionATPL_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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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