4xd7: Difference between revisions
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<StructureSection load='4xd7' size='340' side='right'caption='[[4xd7]], [[Resolution|resolution]] 3.90Å' scene=''> | <StructureSection load='4xd7' size='340' side='right'caption='[[4xd7]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xd7]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4xd7]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._PS3 Bacillus sp. PS3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XD7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand= | </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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4xd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xd7 OCA], [https://pdbe.org/4xd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xd7 RCSB], [https://www.ebi.ac.uk/pdbsum/4xd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xd7 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ATPA_BACP3 ATPA_BACP3] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[HAMAP-Rule:MF_01346] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus sp. PS3]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: NAKASAKO | [[Category: NAKASAKO M]] | ||
[[Category: SHIRAKIHARA | [[Category: SHIRAKIHARA Y]] | ||
[[Category: SHIRATORI | [[Category: SHIRATORI A]] | ||
[[Category: SUZUKI | [[Category: SUZUKI T]] | ||
[[Category: TANIKAWA | [[Category: TANIKAWA H]] | ||
[[Category: YOSHIDA | [[Category: YOSHIDA M]] | ||
Revision as of 00:23, 13 April 2023
Structure of thermophilic F1-ATPase inhibited by epsilon subunitStructure of thermophilic F1-ATPase inhibited by epsilon subunit
Structural highlights
FunctionATPA_BACP3 Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[HAMAP-Rule:MF_01346] Publication Abstract from PubMedF1 -ATPase (F1 ) is the catalytic sector in Fo F1 -ATP synthase that is responsible for ATP production in living cells. In catalysis, its three catalytic beta-subunits undergo nucleotide occupancy-dependent and concerted open-close conformational changes that are accompanied by rotation of the gamma-subunit. Bacterial and chloroplast F1 are inhibited by their own epsilon-subunit. In the epsilon-inhibited Escherichia coli F1 structure, the epsilon-subunit stabilizes the overall conformation (half-closed, closed, open) of the beta-subunits by inserting its C-terminal helix into the alpha3 beta3 cavity. The structure of epsilon-inhibited thermophilic F1 is similar to that of E. coli F1 , showing a similar conformation of the epsilon-subunit, but the thermophilic epsilon-subunit stabilizes another unique overall conformation (open, closed, open) of the beta-subunits. The epsilon-C-terminal helix 2 and hook are conserved between the two structures in interactions with target residues and in their positions. Rest of the epsilon-C-terminal domains are in quite different conformations and positions, and have different modes of interaction with targets. This region is thought to serve epsilon-inhibition differently. For inhibition, the epsilon-subunit contacts the second catches of some of the beta- and alpha-subunits, the N- and C-terminal helices, and some of the Rossmann fold segments. Those contacts, as a whole, lead to positioning of those beta- and alpha- second catches in epsilon-inhibition-specific positions, and prevent rotation of the gamma-subunit. Some of the structural features are observed even in IF1 inhibition in mitochondrial F1 . DATABASE: Structural data are available in the Worldwide Protein Data Bank database under the accession number 4XD7. Structure of a thermophilic F1 -ATPase inhibited by an epsilon-subunit: deeper insight into the epsilon-inhibition mechanism.,Shirakihara Y, Shiratori A, Tanikawa H, Nakasako M, Yoshida M, Suzuki T FEBS J. 2015 Aug;282(15):2895-913. doi: 10.1111/febs.13329. Epub 2015 Jun 19. PMID:26032434[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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