2rgv

From Proteopedia

(Difference between revisions)

Revision as of 07:47, 16 March 2022

The crystal structure of PerR-Ox highlights 2-oxo-Histidine formation

Structural highlights

2rgv is a 2 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	2fe3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PERR_BACSU] Hydrogen and organic peroxide sensor. Represses the expression of a regulon of peroxide-inducible genes such as katA, ahpC, ahpF, the heme biosynthesis operon (hemAXCDBL), fur, perR, zosA and mrgA.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

In Bacillus subtilis, PerR is a metal-dependent sensor of hydrogen peroxide. PerR is a dimeric zinc protein with a regulatory site that coordinates either Fe(2+) (PerR-Zn-Fe) or Mn(2+) (PerR-Zn-Mn). Though most of the peroxide sensors use cysteines to detect H(2)O(2), it has been shown that reaction of PerR-Zn-Fe with H(2)O(2) leads to the oxidation of one histidine residue. Oxidation of PerR leads to the incorporation of one oxygen atom into His37 or His91. This study presents the crystal structure of the oxidized PerR protein (PerR-Zn-ox), which clearly shows a 2-oxo-histidine residue in position 37. Formation of 2-oxo-histidine is demonstrated and quantified by HPLC-MS/MS. EPR experiments indicate that PerR-Zn-H37ox retains a significant affinity for the regulatory metal, whereas PerR-Zn-H91ox shows a considerably reduced affinity for the metal ion. In spite of these major differences in terms of metal binding affinity, oxidation of His37 and/or His91 in PerR prevents DNA binding.

Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein.,Traore DA, El Ghazouani A, Jacquamet L, Borel F, Ferrer JL, Lascoux D, Ravanat JL, Jaquinod M, Blondin G, Caux-Thang C, Duarte V, Latour JM Nat Chem Biol. 2009 Jan;5(1):53-9. Epub 2008 Dec 14. PMID:19079268^[1]

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

References

↑ Traore DA, El Ghazouani A, Jacquamet L, Borel F, Ferrer JL, Lascoux D, Ravanat JL, Jaquinod M, Blondin G, Caux-Thang C, Duarte V, Latour JM. Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein. Nat Chem Biol. 2009 Jan;5(1):53-9. Epub 2008 Dec 14. PMID:19079268 doi:10.1038/nchembio.133

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rgv"

@@ Line 3: / Line 3: @@
 <StructureSection load='2rgv' size='340' side='right'caption='[[2rgv]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2rgv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RGV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2RGV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2rgv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RGV FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OHI:3-(2-OXO-2H-IMIDAZOL-4-YL)-L-ALANINE'>OHI</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fe3|2fe3]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fe3|2fe3]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2rgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rgv OCA], [http://pdbe.org/2rgv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rgv RCSB], [http://www.ebi.ac.uk/pdbsum/2rgv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rgv ProSAT]</span></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=2rgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rgv OCA], [https://pdbe.org/2rgv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rgv RCSB], [https://www.ebi.ac.uk/pdbsum/2rgv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rgv ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PERR_BACSU PERR_BACSU]] Hydrogen and organic peroxide sensor. Represses the expression of a regulon of peroxide-inducible genes such as katA, ahpC, ahpF, the heme biosynthesis operon (hemAXCDBL), fur, perR, zosA and mrgA.
+[[https://www.uniprot.org/uniprot/PERR_BACSU PERR_BACSU]] Hydrogen and organic peroxide sensor. Represses the expression of a regulon of peroxide-inducible genes such as katA, ahpC, ahpF, the heme biosynthesis operon (hemAXCDBL), fur, perR, zosA and mrgA.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2rgv

From Proteopedia

Revision as of 07:47, 16 March 2022

The crystal structure of PerR-Ox highlights 2-oxo-Histidine formation

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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