6y3x
From Proteopedia
(Difference between revisions)
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==Crystal structure of the Francisella novicida lysine decarboxylase LdcF== | ==Crystal structure of the Francisella novicida lysine decarboxylase LdcF== | ||
| - | <StructureSection load='6y3x' size='340' side='right'caption='[[6y3x]]' scene=''> | + | <StructureSection load='6y3x' size='340' side='right'caption='[[6y3x]], [[Resolution|resolution]] 3.40Å' 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=6Y3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y3X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6y3x]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Francisella_tularensis_subsp._novicida Francisella tularensis subsp. novicida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y3X 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=6y3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y3x OCA], [https://pdbe.org/6y3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y3x RCSB], [https://www.ebi.ac.uk/pdbsum/6y3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y3x ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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=6y3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y3x OCA], [https://pdbe.org/6y3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y3x RCSB], [https://www.ebi.ac.uk/pdbsum/6y3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y3x ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0Q584_FRATN A0Q584_FRATN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Francisella tularensis is one of the most virulent pathogenic bacteria causing the acute human respiratory disease tularemia. While the mechanisms underlying F. tularensis pathogenesis are largely unknown, previous studies have shown that a F. novicida transposon mutant with insertions in a gene coding for a putative lysine decarboxylase was attenuated in mouse spleen, suggesting a possible role of its protein product as a virulence factor. Therefore, we set out to structurally and functionally characterize the F. novicida lysine decarboxylase, which we termed LdcF. Here, we investigate the genetic environment of ldcF as well as its evolutionary relationships with other basic AAT-fold amino acid decarboxylase superfamily members, known as key actors in bacterial adaptative stress response and polyamine biosynthesis. We determine the crystal structure of LdcF and compare it with the most thoroughly studied lysine decarboxylase, E. coli LdcI. We analyze the influence of ldcF deletion on bacterial growth under different stress conditions in dedicated growth media, as well as in infected macrophages, and demonstrate its involvement in oxidative stress resistance. Finally, our mass spectrometry-based quantitative proteomic analysis enables identification of 80 proteins with expression levels significantly affected by ldcF deletion, including several DNA repair proteins potentially involved in the diminished capacity of the F. novicida mutant to deal with oxidative stress. Taken together, we uncover an important role of LdcF in F. novicida survival in host cells through participation in oxidative stress response, thereby singling out this previously uncharacterized protein as a potential drug target. | ||
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| + | Structural and functional analysis of the Francisella lysine decarboxylase as a key actor in oxidative stress resistance.,Felix J, Siebert C, Ducassou JN, Nigou J, Garcia PS, Fraudeau A, Huard K, Mas C, Brochier-Armanet C, Coute Y, Gutsche I, Renesto P Sci Rep. 2021 Jan 13;11(1):972. doi: 10.1038/s41598-020-79611-5. PMID:33441661<ref>PMID:33441661</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6y3x" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Francisella tularensis subsp. novicida]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Felix J]] | [[Category: Felix J]] | ||
Current revision
Crystal structure of the Francisella novicida lysine decarboxylase LdcF
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