1c17

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<StructureSection load='1c17' size='340' side='right'caption='[[1c17]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='1c17' size='340' side='right'caption='[[1c17]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1c17]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. The December 2005 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''ATP Synthase'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2005_12 10.2210/rcsb_pdb/mom_2005_12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C17 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1c17]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. The December 2005 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''ATP Synthase'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2005_12 10.2210/rcsb_pdb/mom_2005_12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C17 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c99|1c99]], [[1c0v|1c0v]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1c99|1c99]], [[1c0v|1c0v]]</div></td></tr>
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<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=1c17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c17 OCA], [http://pdbe.org/1c17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c17 RCSB], [http://www.ebi.ac.uk/pdbsum/1c17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1c17 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c17 OCA], [https://pdbe.org/1c17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c17 RCSB], [https://www.ebi.ac.uk/pdbsum/1c17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c17 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ATPL_ECOLI ATPL_ECOLI]] 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/ATP6_ECOLI ATP6_ECOLI]] Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.[HAMAP-Rule:MF_01393]
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[[https://www.uniprot.org/uniprot/ATPL_ECOLI ATPL_ECOLI]] 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/ATP6_ECOLI ATP6_ECOLI]] Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.[HAMAP-Rule:MF_01393]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 10:32, 14 July 2021

A1C12 SUBCOMPLEX OF F1FO ATP SYNTHASE

PDB ID 1c17

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