6o5c: Difference between revisions
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<StructureSection load='6o5c' size='340' side='right'caption='[[6o5c]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='6o5c' size='340' side='right'caption='[[6o5c]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6o5c]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O5C OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6o5c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_serotype_M3 Streptococcus pyogenes serotype M3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O5C FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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]] 3.1Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=6o5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o5c OCA], [https://pdbe.org/6o5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o5c RCSB], [https://www.ebi.ac.uk/pdbsum/6o5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o5c ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H2UTK0_STRP3 A0A0H2UTK0_STRP3] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptococcus pyogenes serotype M3]] | ||
[[Category: | [[Category: Do H]] | ||
[[Category: | [[Category: Kumaraswami M]] | ||
Latest revision as of 10:04, 11 October 2023
X-ray crystal structure of metal-dependent transcriptional regulator MtsRX-ray crystal structure of metal-dependent transcriptional regulator MtsR
Structural highlights
FunctionPublication Abstract from PubMedPathogenic bacteria encounter host-imposed manganese (Mn) limitation during infection. Herein we report that in the human pathogen Streptococcus pyogenes, the adaptive response to Mn limitation is controlled by a DtxR family metalloregulator, MtsR. Genes upregulated by MtsR during Mn limitation include Mn (mtsABC) and Fe acquisition systems (sia operon), and a metal-independent DNA synthesis enzyme (nrdFEI.2). To elucidate the mechanism of metal sensing and gene regulation by MtsR, we determined the crystal structure of MtsR. MtsR employs two Mn-sensing sites to monitor metal availability, and metal occupancy at each site influences MtsR regulatory activity. The site 1 acts as the primary Mn sensing site, and loss of metal at site 1 causes robust upregulation of mtsABC. The vacant site 2 causes partial induction of mtsABC, indicating that site 2 functions as secondary Mn sensing site. Furthermore, we show that the C-terminal FeoA domains of adjacent dimers participate in the oligomerization of MtsR on DNA, and multimerization is critical for MtsR regulatory activity. Finally, the mtsR mutant strains defective in metal sensing and oligomerization are attenuated for virulence in a mouse model of invasive infection, indicating that Mn sensing and gene regulation by MtsR are critical processes during S. pyogenes infection. Metal sensing and regulation of adaptive responses to manganese limitation by MtsR is critical for group A streptococcus virulence.,Do H, Makthal N, Chandrangsu P, Olsen RJ, Helmann JD, Musser JM, Kumaraswami M Nucleic Acids Res. 2019 Jun 12. pii: 5514186. doi: 10.1093/nar/gkz524. PMID:31188450[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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