7p3w
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==F1Fo-ATP synthase from Acinetobacter baumannii (state 3)== | |
| + | <StructureSection load='7p3w' size='340' side='right'caption='[[7p3w]], [[Resolution|resolution]] 4.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7p3w]] 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=7P3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P3W FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.3Å</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></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=7p3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p3w OCA], [https://pdbe.org/7p3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p3w RCSB], [https://www.ebi.ac.uk/pdbsum/7p3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p3w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ATPF_ACIBT ATPF_ACIBT] 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_01398] Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).[HAMAP-Rule:MF_01398] | ||
| + | <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> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7p3w" style="background-color:#fffaf0;"></div> |
| - | [[Category: Bublitz | + | |
| - | [[Category: Demmer | + | ==See Also== |
| - | [[Category: | + | *[[ATPase 3D structures|ATPase 3D structures]] |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Acinetobacter baumannii ATCC 17978]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Allsopp LP]] | ||
| + | [[Category: Bublitz M]] | ||
| + | [[Category: Demmer JK]] | ||
| + | [[Category: Filloux A]] | ||
| + | [[Category: Meier T]] | ||
| + | [[Category: Phillips BP]] | ||
| + | [[Category: Uhrig OL]] | ||
Current revision
F1Fo-ATP synthase from Acinetobacter baumannii (state 3)
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