3v3c: Difference between revisions
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==Crystal Structure of Chloroplast ATP synthase c-ring from Pisum sativum== | |||
<StructureSection load='3v3c' size='340' side='right'caption='[[3v3c]], [[Resolution|resolution]] 3.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3v3c]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V3C 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]] 3.402Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGD:DIGALACTOSYL+DIACYL+GLYCEROL+(DGDG)'>DGD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=YT3:YTTRIUM+(III)+ION'>YT3</scene></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=3v3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v3c OCA], [https://pdbe.org/3v3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v3c RCSB], [https://www.ebi.ac.uk/pdbsum/3v3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v3c ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ATPH_PEA ATPH_PEA] 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 between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396] | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pisum sativum]] | |||
[[Category: Nelson N]] | |||
[[Category: Saroussi S]] | |||
Latest revision as of 10:29, 1 March 2024
Crystal Structure of Chloroplast ATP synthase c-ring from Pisum sativum
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