7p2y: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==== | ==F1Fo-ATP synthase from Acinetobacter baumannii (state 1)== | ||
<StructureSection load='7p2y' size='340' side='right'caption='[[7p2y]]' scene=''> | <StructureSection load='7p2y' size='340' side='right'caption='[[7p2y]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7p2y]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_ATCC_17978 Acinetobacter baumannii ATCC 17978]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P2Y FirstGlance]. <br> | ||
</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=7p2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p2y OCA], [https://pdbe.org/7p2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p2y RCSB], [https://www.ebi.ac.uk/pdbsum/7p2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p2y ProSAT]</span></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]] 3.1Å</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=7p2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p2y OCA], [https://pdbe.org/7p2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p2y RCSB], [https://www.ebi.ac.uk/pdbsum/7p2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p2y ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ATPA_ACIBT ATPA_ACIBT] 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;"> | |||
== Publication Abstract from PubMed == | |||
The global spread of multidrug-resistant Acinetobacter baumannii infections urgently calls for the identification of novel drug targets. We solved the electron cryo-microscopy structure of the F(1)F(o)-adenosine 5'-triphosphate (ATP) synthase from A. baumannii in three distinct conformational states. The nucleotide-converting F(1) subcomplex reveals a specific self-inhibition mechanism, which supports a unidirectional ratchet mechanism to avoid wasteful ATP consumption. In the membrane-embedded F(o) complex, the structure shows unique structural adaptations along both the entry and exit pathways of the proton-conducting a-subunit. These features, absent in mitochondrial ATP synthases, represent attractive targets for the development of next-generation therapeutics that can act directly at the culmination of bioenergetics in this clinically relevant pathogen. | |||
Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii.,Demmer JK, Phillips BP, Uhrig OL, Filloux A, Allsopp LP, Bublitz M, Meier T Sci Adv. 2022 Feb 18;8(7):eabl5966. doi: 10.1126/sciadv.abl5966. Epub 2022 Feb , 16. PMID:35171679<ref>PMID:35171679</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7p2y" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Acinetobacter baumannii ATCC 17978]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Allsopp LP]] | ||
[[Category: Bublitz M]] | |||
[[Category: Demmer JK]] | |||
[[Category: Filloux A]] | |||
[[Category: Meier T]] | |||
[[Category: Phillips BP]] | |||
[[Category: Uhrig OL]] | |||
Latest revision as of 12:30, 17 July 2024
F1Fo-ATP synthase from Acinetobacter baumannii (state 1)
| ||||||||||||
