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2wie
From Proteopedia
(Difference between revisions)
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| - | + | ==HIGH-RESOLUTION STRUCTURE OF THE ROTOR RING FROM A PROTON DEPENDENT ATP SYNTHASE== | |
| - | + | <StructureSection load='2wie' size='340' side='right' caption='[[2wie]], [[Resolution|resolution]] 2.13Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2wie]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WIE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WIE FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CVM:CYMAL-4'>CVM</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wie OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wie RCSB], [http://www.ebi.ac.uk/pdbsum/2wie PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wi/2wie_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The crystal structure of the c-ring from the proton-coupled F1Fo ATP synthase from Spirulina platensis is shown at 2.1-A resolution. The ring includes 15 membrane-embedded c subunits forming an hourglass-shaped assembly. The structure demonstrates that proton translocation across the membrane entails protonation of a conserved glutamate located near the membrane center in the c subunit outer helix. The proton is locked in this site by a precise hydrogen bond network reminiscent of that in Na+-dependent ATP synthases. However, the structure suggests that the different coordination chemistry of the bound proton and the smaller curvature of the outer helix drastically enhance the selectivity of the H+ site against other cations, including H3O+. We propose a model for proton translocation whereby the c subunits remain in this proton-locked state when facing the membrane lipid. Proton exchange would occur in a more hydrophilic and electrostatically distinct environment upon contact with the a subunit interface. | ||
| - | + | High-resolution structure of the rotor ring of a proton-dependent ATP synthase.,Pogoryelov D, Yildiz O, Faraldo-Gomez JD, Meier T Nat Struct Mol Biol. 2009 Oct;16(10):1068-73. Epub 2009 Sep 27. PMID:19783985<ref>PMID:19783985</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | |||
| + | ==See Also== | ||
| + | *[[ATPase|ATPase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Arthrospira platensis]] | [[Category: Arthrospira platensis]] | ||
[[Category: Faraldo-Gomez, J D.]] | [[Category: Faraldo-Gomez, J D.]] | ||
Revision as of 02:03, 1 October 2014
HIGH-RESOLUTION STRUCTURE OF THE ROTOR RING FROM A PROTON DEPENDENT ATP SYNTHASE
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Categories: Arthrospira platensis | Faraldo-Gomez, J D. | Meier, T. | Pogoryelov, D. | Yildiz, O. | C-ring structure | F1fo atp synthase rotor | Hydrogen ion transport | Hydrolase | Ion proton-translocation | Ion transport | Lipid-binding | Membrane | Membrane protein complex | Spirulina platensis | Transmembrane

