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==STRUCTURE OF ALA24/ASP61 TO ASP24/ASN61 SUBSTITUTED SUBUNIT C OF ESCHERICHIA COLI ATP SYNTHASE==
==STRUCTURE OF ALA24/ASP61 TO ASP24/ASN61 SUBSTITUTED SUBUNIT C OF ESCHERICHIA COLI ATP SYNTHASE==
<StructureSection load='1l6t' size='340' side='right'caption='[[1l6t]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='1l6t' size='340' side='right'caption='[[1l6t]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1l6t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L6T FirstGlance]. <br>
<table><tr><td colspan='2'>[[1l6t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L6T FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1c0v|1c0v]], [[1c99|1c99]]</div></td></tr>
</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uncE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Iron-chelate-transporting_ATPase Iron-chelate-transporting ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.34 3.6.3.34] </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=1l6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l6t OCA], [https://pdbe.org/1l6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l6t RCSB], [https://www.ebi.ac.uk/pdbsum/1l6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l6t 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=1l6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l6t OCA], [https://pdbe.org/1l6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l6t RCSB], [https://www.ebi.ac.uk/pdbsum/1l6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l6t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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/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]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Iron-chelate-transporting ATPase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Abildgaard, F]]
[[Category: Abildgaard F]]
[[Category: Dmitriev, O Y]]
[[Category: Dmitriev OY]]
[[Category: Fillingame, R H]]
[[Category: Fillingame RH]]
[[Category: Markley, J L]]
[[Category: Markley JL]]
[[Category: Hydrolase]]
[[Category: Transmembrane helix]]
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