9t9n: Difference between revisions

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'''Unreleased structure'''


The entry 9t9n is ON HOLD  until 2027-11-17
==Crystal structure of Ap4A Hydrolase (ApaH) from Pseudomonas aeruginosa in complex with Mg ions==
<StructureSection load='9t9n' size='340' side='right'caption='[[9t9n]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9t9n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9T9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9T9N FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=9t9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9t9n OCA], [https://pdbe.org/9t9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9t9n RCSB], [https://www.ebi.ac.uk/pdbsum/9t9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9t9n ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/APAH_PSEAE APAH_PSEAE] Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Infections by Pseudomonas aeruginosa are a major cause of severe morbidity and mortality in immunocompromised patients and people with cystic fibrosis, largely due to the pathogen's ability to resist antibiotic treatment and to deploy multiple virulence strategies that promote persistence in the host. We have recently uncovered that the signaling molecule diadenosine tetraphosphate (Ap4A) acts as a crucial regulator of P. aeruginosa virulence. Specifically, deletion of the Ap4A-degrading enzyme, diadenosine tetraphosphatase (ApaH), dramatically reduces the expression of key virulence factors. The structural and molecular properties of P. aeruginosa ApaH (PaApaH) remain uncharacterized. Here, we present an integrated biochemical, structural, computational, and phenotypic characterization of PaApaH. We define the molecular determinants of its manganese-dependent Ap4A hydrolytic mechanism and establish a direct functional link between PaApaH catalytic activity and virulence phenotypes in vivo. Together with the absence of ApaH homologs in eukaryotes, these findings place PaApaH as an attractive and selective target for antivirulence therapeutic strategies against P. aeruginosa infections.


Authors: Pistoia, G., Imperi, F., Di Matteo, A., Giardina, G.
Structural and functional insights into Pseudomonas aeruginosa ApaH, a diadenosine tetraphosphatase crucial for bacterial virulence.,Pistoia G, Cervoni M, Catalano F, Troilo F, Guidi F, Comparini E, Mignogna G, Travaglini-Allocatelli C, Giuffre A, Coluccia A, Imperi F, Di Matteo A, Giardina G Protein Sci. 2026 Sep;35(9):e70781. doi: 10.1002/pro.70781. PMID:42640267<ref>PMID:42640267</ref>


Description: Crystal structure of Ap4A Hydrolase (ApaH) from Pseudomonas aeruginosa in complex with Mg ions
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Di Matteo, A]]
<div class="pdbe-citations 9t9n" style="background-color:#fffaf0;"></div>
[[Category: Pistoia, G]]
== References ==
[[Category: Giardina, G]]
<references/>
[[Category: Imperi, F]]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Di Matteo A]]
[[Category: Giardina G]]
[[Category: Imperi F]]
[[Category: Pistoia G]]