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| | <StructureSection load='4mjn' size='340' side='right'caption='[[4mjn]], [[Resolution|resolution]] 6.00Å' scene=''> | | <StructureSection load='4mjn' size='340' side='right'caption='[[4mjn]], [[Resolution|resolution]] 6.00Å' scene=''> |
| | == Structural highlights == | | == 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> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2w5j|2w5j]]</td></tr> | + | </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> |
| - | <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>
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| - | <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://pdbe.org/4mjn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mjn RCSB], [http://www.ebi.ac.uk/pdbsum/4mjn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mjn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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). | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Triticum aestivum]] | | [[Category: Triticum aestivum]] |
| - | [[Category: Balakrishna, A M]] | + | [[Category: Balakrishna AM]] |
| - | [[Category: Gruber, G]] | + | [[Category: Gruber G]] |
| - | [[Category: Hydrolase]]
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| Structural highlights
Function
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).
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Balakrishna AM, Seelert H, Marx SH, Dencher NA, Gruber G. Crystallographic structure of the turbine C-ring from spinach chloroplast F-ATP synthase. Biosci Rep. 2014 Apr 1;34(2). pii: BSR20130114. doi: 10.1042/BSR20130114. Print, 2014 Apr 1. PMID:27919036 doi:http://dx.doi.org/10.1042/BSR20130114
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