6o5c

X-ray crystal structure of metal-dependent transcriptional regulator MtsR

spinqualitylabelsall models 6o5c, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6o5c is a 2 chain structure with sequence from Streptococcus pyogenes serotype M3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: MN, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2UTK0_STRP3 Publication Abstract from PubMed Pathogenic 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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