4mjn
From Proteopedia
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| - | + | ==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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MJN FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2w5j|2w5j]]</td></tr> |
| + | <tr id='activity'><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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mjn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mjn RCSB], [http://www.ebi.ac.uk/pdbsum/4mjn PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://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). | [[http://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 adenosine triphosphate (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 masculine and diffracted to 4.5 A resolution. Each c-ring contains fourteen 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 Feb 13. PMID:24521269<ref>PMID:24521269</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Triticum aestivum]] | [[Category: Triticum aestivum]] | ||
| - | [[Category: Balakrishna, A M | + | [[Category: Balakrishna, A M]] |
| - | [[Category: Gruber, G | + | [[Category: Gruber, G]] |
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 16:40, 24 December 2014
Structure of the c ring of the CF1FO ATP synthases.
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