6a07: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Salmonella Typhi YfdX in the F222 space group at 1.5 A resolution== | ==Salmonella Typhi YfdX in the F222 space group at 1.5 A resolution== | ||
<StructureSection load='6a07' size='340' side='right' caption='[[6a07]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='6a07' size='340' side='right'caption='[[6a07]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6a07]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A07 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6a07]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A07 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6a07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a07 OCA], [https://pdbe.org/6a07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a07 RCSB], [https://www.ebi.ac.uk/pdbsum/6a07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a07 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 16: | Line 16: | ||
</div> | </div> | ||
<div class="pdbe-citations 6a07" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6a07" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[YfdX|YfdX]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Kim, S J]] | [[Category: Kim, S J]] | ||
[[Category: Ku, B]] | [[Category: Ku, B]] | ||
Revision as of 13:13, 18 March 2021
Salmonella Typhi YfdX in the F222 space group at 1.5 A resolutionSalmonella Typhi YfdX in the F222 space group at 1.5 A resolution
Structural highlights
Publication Abstract from PubMedYfdX is a prokaryotic protein encoded by several pathogenic bacteria including Salmonella enterica serovar Typhi, which causes one of the most fatal infectious diseases, typhoid fever. YfdX is a product of the yfdXWUVE operon and is known to be under the control of EvgA, a regulator protein controlling the expression of several proteins involved in response to environmental stress, in Escherichia coli. Nevertheless, unlike other proteins encoded by the same operon, the structural and physiological aspects of YfdX have been poorly characterized. Here, we identified a previously unknown pH-dependent stoichiometric conversion of S. Typhi YfdX between dimeric and tetrameric states; this conversion was further analyzed via determining its structure by X-ray crystallography at high resolution and by small-angle X-ray scattering in a solution state and via structure-based mutant studies. Biologically, YfdX was proven to be critically involved in Salmonella susceptibility to two beta-lactam antibiotics, penicillin G and carbenicillin, as bacterial growth significantly impaired by its deficiency upon treatment with each of the two antibiotics was recovered by chromosomal complementation. Furthermore, by using Galleria mellonella larvae as an in vivo model of Salmonella infection, we demonstrated that Salmonella virulence was remarkably enhanced by YfdX deficiency, which was complemented by a transient expression of the wild-type or dimeric mutant but not by that of the monomeric mutant. The present study work provides direct evidence regarding the participation of YfdX in Salmonella antibiotic susceptibility and in the modulation of bacterial virulence, providing a new insight into this pathogen's strategies for survival and growth. Structural and Physiological Exploration of Salmonella Typhi YfdX Uncovers Its Dual Function in Bacterial Antibiotic Stress and Virulence.,Lee HS, Lee S, Kim JS, Lee HR, Shin HC, Lee MS, Jin KS, Kim CH, Ku B, Ryu CM, Kim SJ Front Microbiol. 2019 Jan 14;9:3329. doi: 10.3389/fmicb.2018.03329. eCollection, 2018. PMID:30692978[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||