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2w5j

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[[Image:2w5j.png|left|200px]]
 
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{{STRUCTURE_2w5j| PDB=2w5j | SCENE= }}
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==Structure of the c14-rotor ring of the proton translocating chloroplast ATP synthase==
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<StructureSection load='2w5j' size='340' side='right'caption='[[2w5j]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2w5j]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W5J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W5J FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8&#8491;</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=2w5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w5j OCA], [https://pdbe.org/2w5j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w5j RCSB], [https://www.ebi.ac.uk/pdbsum/2w5j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w5j ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ATPH_SPIOL ATPH_SPIOL] 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 14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w5/2w5j_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2w5j ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of the membrane integral rotor ring of the proton translocating F(1)F(0) ATP synthase from spinach chloroplasts was determined to 3.8 A resolution by x-ray crystallography. The rotor ring consists of 14 identical protomers that are symmetrically arranged around a central pore. Comparisons with the c(11) rotor ring of the sodium translocating ATPase from Ilyobacter tartaricus show that the conserved carboxylates involved in proton or sodium transport, respectively, are 10.6-10.8 A apart in both c ring rotors. This finding suggests that both ATPases have the same gear distance despite their different stoichiometries. The putative proton-binding site at the conserved carboxylate Glu(61) in the chloroplast ATP synthase differs from the sodium-binding site in Ilyobacter. Residues adjacent to the conserved carboxylate show increased hydrophobicity and reduced hydrogen bonding. The crystal structure reflects the protonated form of the chloroplast c ring rotor. We propose that upon deprotonation, the conformation of Glu(61) is changed to another rotamer and becomes fully exposed to the periphery of the ring. Reprotonation of Glu(61) by a conserved arginine in the adjacent a subunit returns the carboxylate to its initial conformation.
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===STRUCTURE OF THE C14-ROTOR RING OF THE PROTON TRANSLOCATING CHLOROPLAST ATP SYNTHASE===
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Structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase.,Vollmar M, Schlieper D, Winn M, Buchner C, Groth G J Biol Chem. 2009 Jul 3;284(27):18228-35. Epub 2009 May 7. PMID:19423706<ref>PMID:19423706</ref>
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{{ABSTRACT_PUBMED_19423706}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 2w5j" style="background-color:#fffaf0;"></div>
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[[2w5j]] is a 14 chain structure of [[ATP synthase]] with sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W5J OCA].
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==See Also==
==See Also==
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*[[ATP synthase|ATP synthase]]
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*[[ATPase 3D structures|ATPase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:019423706</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Spinacia oleracea]]
[[Category: Spinacia oleracea]]
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[[Category: Buechner, C.]]
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[[Category: Buechner C]]
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[[Category: Groth, G.]]
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[[Category: Groth G]]
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[[Category: Schlieper, D.]]
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[[Category: Schlieper D]]
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[[Category: Vollmar, M.]]
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[[Category: Vollmar M]]
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[[Category: Winn, M.]]
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[[Category: Winn M]]
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[[Category: Atp synthase]]
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[[Category: Chloroplast]]
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[[Category: Energy transduction]]
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[[Category: Formylation]]
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[[Category: Hydrogen ion transport]]
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[[Category: Hydrolase]]
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[[Category: Ion transport]]
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[[Category: Lipid-binding]]
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[[Category: Membrane]]
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[[Category: Membrane protein]]
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[[Category: Transmembrane]]
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[[Category: Transport]]
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Current revision

Structure of the c14-rotor ring of the proton translocating chloroplast ATP synthase

PDB ID 2w5j

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