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2khk
From Proteopedia
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==NMR solution structure of the b30-82 domain of subunit b of Escherichia coli F1FO ATP synthase== | ==NMR solution structure of the b30-82 domain of subunit b of Escherichia coli F1FO ATP synthase== | ||
| - | <StructureSection load='2khk' size='340' side='right' caption='[[2khk | + | <StructureSection load='2khk' size='340' side='right'caption='[[2khk]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2khk]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2khk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KHK FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </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=2khk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2khk OCA], [https://pdbe.org/2khk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2khk RCSB], [https://www.ebi.ac.uk/pdbsum/2khk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2khk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ATPF_ECOLI ATPF_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 (By similarity).<ref>PMID:1682301</ref> Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0) (By similarity).<ref>PMID:1682301</ref> |
== 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/kh/2khk_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kh/2khk_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=2khk ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 2khk" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[ATPase|ATPase]] | + | *[[ATPase 3D structures|ATPase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Escherichia coli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Biukovic | + | [[Category: Large Structures]] |
| - | [[Category: Gayen | + | [[Category: Biukovic G]] |
| - | [[Category: Gruber | + | [[Category: Gayen S]] |
| - | [[Category: Priya | + | [[Category: Gruber G]] |
| - | [[Category: Vivekanandan | + | [[Category: Priya R]] |
| - | + | [[Category: Vivekanandan S]] | |
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Current revision
NMR solution structure of the b30-82 domain of subunit b of Escherichia coli F1FO ATP synthase
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