8ap9
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8ap9]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AP9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8ap9]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AP9 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</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=8ap9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ap9 OCA], [https://pdbe.org/8ap9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ap9 RCSB], [https://www.ebi.ac.uk/pdbsum/8ap9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ap9 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=8ap9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ap9 OCA], [https://pdbe.org/8ap9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ap9 RCSB], [https://www.ebi.ac.uk/pdbsum/8ap9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ap9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/ | + | [https://www.uniprot.org/uniprot/ATPG_TRYBB ATPG_TRYBB] Mitochondrial membrane ATP synthase (F(1)F(o) ATP synthase) 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 (PubMed:19436713, PubMed:29247468). F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(o) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:19436713, PubMed:29247468, PubMed:29440423). 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) (PubMed:19436713, PubMed:29440423). 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 (Probable). Contrary to the procyclic, insect form that requires F(1)F(o) ATP synthase for ATP synthesis, the bloodstream form relies on ATP hydrolysis by F(1)F(o) ATP synthase to maintain its mitochondrial membrane potential (PubMed:29247468).<ref>PMID:19436713</ref> <ref>PMID:29247468</ref> <ref>PMID:29440423</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Current revision
rotor of the Trypanosoma brucei mitochondrial ATP synthase dimer
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