7p3w: Difference between revisions

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====
==F1Fo-ATP synthase from Acinetobacter baumannii (state 3)==
<StructureSection load='7p3w' size='340' side='right'caption='[[7p3w]]' scene=''>
<StructureSection load='7p3w' size='340' side='right'caption='[[7p3w]], [[Resolution|resolution]] 4.30&Aring;' 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'>[[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='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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.3&#8491;</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>
</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7p3w" 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: Z-disk]]
[[Category: Allsopp LP]]
[[Category: Bublitz M]]
[[Category: Demmer JK]]
[[Category: Filloux A]]
[[Category: Meier T]]
[[Category: Phillips BP]]
[[Category: Uhrig OL]]
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