8vsq: Difference between revisions
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==Crystal structure of Esub1== | |||
<StructureSection load='8vsq' size='340' side='right'caption='[[8vsq]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8vsq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_MGAS315 Streptococcus pyogenes MGAS315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VSQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VSQ 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]] 2.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8vsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vsq OCA], [https://pdbe.org/8vsq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vsq RCSB], [https://www.ebi.ac.uk/pdbsum/8vsq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vsq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H2UUU0_STRP3 A0A0H2UUU0_STRP3] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Streptococcus pyogenes, or Group A Streptococcus (GAS), is a commensal bacteria and human pathogen. Central to GAS pathogenesis is the presence of prophage encoded virulence genes. The conserved phage gene for the protein paratox (Prx) is genetically linked to virulence genes, but the reason for this linkage is unknown. Prx inhibits GAS quorum sensing and natural competence by binding the transcription factor ComR. However, inhibiting ComR does not explain the virulence gene linkage. To address this, we took a mass spectrometry approach to search for other Prx interaction partners. The data demonstrates that Prx binds numerous DNA-binding proteins and transcriptional regulators. We show binding of Prx in vitro with the GAS protein Esub1 (SpyM3_0890) and the phage protein JM3 (SpyM3_1246). An Esub1:Prx complex X-ray crystal structure reveals that Esub1 and ComR possess a conserved Prx-binding helix. Computational modelling predicts that the Prx-binding helix is present in several, but not all, binding partners. Namely, JM3 lacks the Prx-binding helix. As Prx is conformationally dynamic, this suggests partner-dependent binding modes. Overall, Prx acts as a metabolic regulator of GAS to maintain the phage genome. As such, Prx maybe a direct contributor to the pathogenic conversion of GAS. | |||
The phage protein paratox is a multifunctional metabolic regulator of Streptococcus.,Muna TH, Rutbeek NR, Horne J, Lao YW, Krokhin OV, Prehna G Nucleic Acids Res. 2024 Dec 14:gkae1200. doi: 10.1093/nar/gkae1200. PMID:39673798<ref>PMID:39673798</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8vsq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus pyogenes MGAS315]] | |||
[[Category: Muna TH]] | |||
[[Category: Prehna G]] | |||
Latest revision as of 10:56, 9 January 2025
Crystal structure of Esub1Crystal structure of Esub1
Structural highlights
FunctionPublication Abstract from PubMedStreptococcus pyogenes, or Group A Streptococcus (GAS), is a commensal bacteria and human pathogen. Central to GAS pathogenesis is the presence of prophage encoded virulence genes. The conserved phage gene for the protein paratox (Prx) is genetically linked to virulence genes, but the reason for this linkage is unknown. Prx inhibits GAS quorum sensing and natural competence by binding the transcription factor ComR. However, inhibiting ComR does not explain the virulence gene linkage. To address this, we took a mass spectrometry approach to search for other Prx interaction partners. The data demonstrates that Prx binds numerous DNA-binding proteins and transcriptional regulators. We show binding of Prx in vitro with the GAS protein Esub1 (SpyM3_0890) and the phage protein JM3 (SpyM3_1246). An Esub1:Prx complex X-ray crystal structure reveals that Esub1 and ComR possess a conserved Prx-binding helix. Computational modelling predicts that the Prx-binding helix is present in several, but not all, binding partners. Namely, JM3 lacks the Prx-binding helix. As Prx is conformationally dynamic, this suggests partner-dependent binding modes. Overall, Prx acts as a metabolic regulator of GAS to maintain the phage genome. As such, Prx maybe a direct contributor to the pathogenic conversion of GAS. The phage protein paratox is a multifunctional metabolic regulator of Streptococcus.,Muna TH, Rutbeek NR, Horne J, Lao YW, Krokhin OV, Prehna G Nucleic Acids Res. 2024 Dec 14:gkae1200. doi: 10.1093/nar/gkae1200. PMID:39673798[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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