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4i7h

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Revision as of 08:46, 9 November 2022

Structural basis for peroxide sensing and gene regulation by PerR from Streptococcus pyogenes

Structural highlights

4i7h is a 2 chain structure with sequence from Streptococcus pyogenes MGAS315. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A0H2UT39_STRP3

Publication Abstract from PubMed

Regulation of oxidative stress responses by peroxide stress regulator (PerR) is critical for the in vivo fitness and virulence of group A Streptococcus (GAS). To elucidate the molecular mechanism of DNA binding, peroxide sensing, and gene regulation by PerR, we performed biochemical and structural characterization of PerR. Sequence-specific DNA binding by PerR does not require regulatory metal occupancy. However, metal binding promotes higher affinity PerR-DNA interactions. PerR metallated with iron directly senses peroxide stress and dissociates from operator sequences. The crystal structure revealed that PerR exists as a homodimer with two metal binding sites per subunit: a structural zinc site and a regulatory metal site that is occupied in the crystals by nickel. The regulatory metal-binding site in PerR involves a previously unobserved H-X-H motif located in its unique N-terminal extension. Mutational analysis of the regulatory site showed that the PerR metal ligands are involved in regulatory metal binding and integrity of this site is critical for GAS virulence. Interestingly, the metal-binding H-X-H motif is not present in the structurally characterized members of Ferric uptake regulator (Fur) family but fully conserved among PerR from the genus Streptococcus. Thus, it is likely that the PerR orthologs from streptococci share a common mechanism of metal binding, peroxide sensing, and gene regulation that is different from that of well-characterized PerR from Bacillus subtilis. Together, our findings provide key insights into the peroxide sensing and regulation of the oxidative stress adaptive responses by the streptococcal subfamily of PerR.

Crystal structure of peroxide stress regulator (PerR) from Streptococcus pyogenes provides functional insights into the mechanism of oxidative stress sensing.,Makthal N, Rastegari S, Sanson M, Ma Z, Olsen RJ, Helmann JD, Musser JM, Kumaraswami M J Biol Chem. 2013 May 3. PMID:23645680^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Makthal N, Rastegari S, Sanson M, Ma Z, Olsen RJ, Helmann JD, Musser JM, Kumaraswami M. Crystal structure of peroxide stress regulator (PerR) from Streptococcus pyogenes provides functional insights into the mechanism of oxidative stress sensing. J Biol Chem. 2013 May 3. PMID:23645680 doi:10.1074/jbc.M113.456590

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4i7h"

Categories: Large Structures | Streptococcus pyogenes MGAS315 | Kumaraswami M

@@ Line 3: / Line 3: @@
 <StructureSection load='4i7h' size='340' side='right'caption='[[4i7h]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4i7h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Strp3 Strp3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I7H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I7H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4i7h]] 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=4I7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I7H FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spf, SpyM3_0147 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=198466 STRP3])</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=4i7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i7h OCA], [https://pdbe.org/4i7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i7h RCSB], [https://www.ebi.ac.uk/pdbsum/4i7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i7h ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4i7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i7h OCA], [http://pdbe.org/4i7h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i7h RCSB], [http://www.ebi.ac.uk/pdbsum/4i7h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i7h ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A0H2UT39_STRP3 A0A0H2UT39_STRP3]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Strp3]]
+[[Category: Streptococcus pyogenes MGAS315]]
-[[Category: Kumaraswami, M]]
+[[Category: Kumaraswami M]]
-[[Category: Dna]]
-[[Category: Metal homeostasis]]
-[[Category: Oxidative stress sensing]]
-[[Category: Transcription]]
-[[Category: Winged helix-turn-helix motif]]

4i7h

From Proteopedia

Revision as of 08:46, 9 November 2022

Structural basis for peroxide sensing and gene regulation by PerR from Streptococcus pyogenes

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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