4mjn
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the c ring of the CF1FO ATP synthases.== | |
| + | <StructureSection load='4mjn' size='340' side='right'caption='[[4mjn]], [[Resolution|resolution]] 6.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4mjn]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MJN FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 6Å</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=4mjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mjn OCA], [https://pdbe.org/4mjn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mjn RCSB], [https://www.ebi.ac.uk/pdbsum/4mjn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mjn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ATPH_WHEAT ATPH_WHEAT] 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). 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 (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In eukaryotic and prokaryotic cells, F-ATP synthases provide energy through the synthesis of ATP. The chloroplast F-ATP synthase (CF1FO-ATP synthase) of plants is integrated into the thylakoid membrane via its FO-domain subunits a, b, b' and c Subunit c with a stoichiometry of 14 and subunit a form the gate for H(+)-pumping, enabling the coupling of electrochemical energy with ATP synthesis in the F1 sector.Here we report the crystallization and structure determination of the c14-ring of subunit c of the CF1FO-ATP synthase from spinach chloroplasts. The crystals belonged to space group C2, with unit-cell parameters a=144.420, b=99.295, c=123.51 A, and beta=104.34 degrees and diffracted to 4.5 A resolution. Each c-ring contains 14 monomers in the asymmetric unit. The length of the c-ring is 60.32 A, with an outer ring diameter 52.30 A and an inner ring width of 40 A. | ||
| - | + | Crystallographic structure of the turbine C-ring from spinach chloroplast F-ATP synthase.,Balakrishna AM, Seelert H, Marx SH, Dencher NA, Gruber G Biosci Rep. 2014 Apr 1;34(2). pii: BSR20130114. doi: 10.1042/BSR20130114. Print, 2014 Apr 1. PMID:27919036<ref>PMID:27919036</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4mjn" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[ATPase 3D structures|ATPase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Triticum aestivum]] | ||
| + | [[Category: Balakrishna AM]] | ||
| + | [[Category: Gruber G]] | ||
Current revision
Structure of the c ring of the CF1FO ATP synthases.
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