2w6e: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2w6e]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W6E FirstGlance]. <br>
<table><tr><td colspan='2'>[[2w6e]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W6E FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 6.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2jiz|2jiz]], [[2v7q|2v7q]], [[1nbm|1nbm]], [[1bmf|1bmf]], [[2jj1|2jj1]], [[1e1q|1e1q]], [[1w0j|1w0j]], [[1cow|1cow]], [[1h8h|1h8h]], [[1e1r|1e1r]], [[1ohh|1ohh]], [[1qo1|1qo1]], [[2jdi|2jdi]], [[1h8e|1h8e]], [[1efr|1efr]], [[2jj2|2jj2]], [[1e79|1e79]], [[2ck3|2ck3]], [[1w0k|1w0k]], [[2w6g|2w6g]], [[2w6i|2w6i]], [[2w6j|2w6j]], [[2w6f|2w6f]], [[2w6h|2w6h]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2w6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6e OCA], [https://pdbe.org/2w6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w6e RCSB], [https://www.ebi.ac.uk/pdbsum/2w6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w6e ProSAT]</span></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=2w6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w6e OCA], [https://pdbe.org/2w6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w6e RCSB], [https://www.ebi.ac.uk/pdbsum/2w6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w6e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ATPA_BOVIN ATPA_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). [[https://www.uniprot.org/uniprot/ATPG_BOVIN ATPG_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. [[https://www.uniprot.org/uniprot/ATPB_BOVIN ATPB_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.  
[https://www.uniprot.org/uniprot/ATPB_BOVIN ATPB_BOVIN] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bowler, M W]]
[[Category: Bowler MW]]
[[Category: Cipriani, F]]
[[Category: Cipriani F]]
[[Category: Felisaz, F]]
[[Category: Felisaz F]]
[[Category: Gobbo, A]]
[[Category: Gobbo A]]
[[Category: Huet, J]]
[[Category: Huet J]]
[[Category: Ravelli, R B.G]]
[[Category: Ravelli RBG]]
[[Category: Sanchez-Weatherby, J]]
[[Category: Sanchez-Weatherby J]]
[[Category: Atp synthesis]]
[[Category: F1fo atp phosphorylase]]
[[Category: Hydrogen ion transport]]
[[Category: Hydrolase]]
[[Category: Ion transport]]
[[Category: P-loop]]
[[Category: Pyrrolidone carboxylic acid]]
[[Category: Transit peptide]]
[[Category: Ubl conjugation]]

Latest revision as of 15:45, 13 December 2023

Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration:hydration state 1.

2w6e, resolution 6.50Å

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