6vwk: Difference between revisions
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<StructureSection load='6vwk' size='340' side='right'caption='[[6vwk]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='6vwk' size='340' side='right'caption='[[6vwk]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6vwk]] is a 13 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6vwk]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VWK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VWK FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">atpE, ECJG_03465 ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">atpE, ECJG_03465 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), atpf ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), atpB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vwk OCA], [https://pdbe.org/6vwk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vwk RCSB], [https://www.ebi.ac.uk/pdbsum/6vwk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vwk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/F4TL55_ECOLX F4TL55_ECOLX]] 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 between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396] [[https://www.uniprot.org/uniprot/C3SL77_ECOLX C3SL77_ECOLX]] Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.[HAMAP-Rule:MF_01393][RuleBase:RU000483] [[https://www.uniprot.org/uniprot/D6IFY0_ECOLX D6IFY0_ECOLX]] Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).[HAMAP-Rule:MF_01398][SAAS:SAAS00535352] 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_01398][SAAS:SAAS00002149] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||