2iy4

From Proteopedia

(Difference between revisions)

Revision as of 07:56, 19 January 2022

X-ray structure of Dps from Listeria monocytogenes

Structural highlights

2iy4 is a 24 chain structure with sequence from "bacterium_monocytogenes_hominis"_nyfeldt_1932 "bacterium monocytogenes hominis" nyfeldt 1932. 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

[DPS_LISMO] Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction. Does not bind to DNA (By similarity). Dps is important for full resistance to heat and cold shocks and is essential for full virulence of this bacterium. It seems to play a direct or indirect role on the production and/or stability of listeriolysin O.^[1] ^[2] ^[3]

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

The stability of the dodecameric Listeria monocytogenes Dps has been compared with that of the Listeria innocua protein. The two proteins differ only in two amino acid residues that form an intersubunit salt-bridge in L. innocua Dps. This salt-bridge is replaced by a hydrogen bonding network in L. monocytogenes Dps as revealed by the X-ray crystal structure. The resistance to low pH and high temperature was assayed for both Dps proteins under equilibrium conditions and kinetically. Despite the identical equilibrium behavior, significant differences in the kinetic stability and activation energy of the unfolding process are apparent at pH 1.5. The higher stability of L. monocytogenes Dps has been accounted for in terms of the persistence of the hydrogen bonding network at this low pH value. In contrast, the salt-bridge between Lys 114 and Asp 126 characteristic of L. innocua Dps is most likely abolished due to protonation of Asp 126.

The mutations Lys 114 --> Gln and Asp 126 --> Asn disrupt an intersubunit salt bridge and convert Listeria innocua Dps into its natural mutant Listeria monocytogenes Dps. Effects on protein stability at Low pH.,Bellapadrona G, Chiaraluce R, Consalvi V, Ilari A, Stefanini S, Chiancone E Proteins. 2007 Mar 1;66(4):975-83. PMID:17186524^[4]

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

References

↑ Polidoro M, De Biase D, Montagnini B, Guarrera L, Cavallo S, Valenti P, Stefanini S, Chiancone E. The expression of the dodecameric ferritin in Listeria spp. is induced by iron limitation and stationary growth phase. Gene. 2002 Aug 21;296(1-2):121-8. PMID:12383509
↑ Olsen KN, Larsen MH, Gahan CG, Kallipolitis B, Wolf XA, Rea R, Hill C, Ingmer H. The Dps-like protein Fri of Listeria monocytogenes promotes stress tolerance and intracellular multiplication in macrophage-like cells. Microbiology. 2005 Mar;151(Pt 3):925-33. PMID:15758237 doi:http://dx.doi.org/151/3/925
↑ Dussurget O, Dumas E, Archambaud C, Chafsey I, Chambon C, Hebraud M, Cossart P. Listeria monocytogenes ferritin protects against multiple stresses and is required for virulence. FEMS Microbiol Lett. 2005 Sep 15;250(2):253-61. PMID:16098690 doi:http://dx.doi.org/10.1016/j.femsle.2005.07.015
↑ Bellapadrona G, Chiaraluce R, Consalvi V, Ilari A, Stefanini S, Chiancone E. The mutations Lys 114 --> Gln and Asp 126 --> Asn disrupt an intersubunit salt bridge and convert Listeria innocua Dps into its natural mutant Listeria monocytogenes Dps. Effects on protein stability at Low pH. Proteins. 2007 Mar 1;66(4):975-83. PMID:17186524 doi:10.1002/prot.21305

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2iy4"

@@ Line 3: / Line 3: @@
 <StructureSection load='2iy4' size='340' side='right'caption='[[2iy4]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2iy4]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_monocytogenes_hominis"_nyfeldt_1932 "bacterium monocytogenes hominis" nyfeldt 1932]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IY4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2IY4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2iy4]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_monocytogenes_hominis"_nyfeldt_1932 "bacterium monocytogenes hominis" nyfeldt 1932]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IY4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IY4 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=2iy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iy4 OCA], [http://pdbe.org/2iy4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iy4 RCSB], [http://www.ebi.ac.uk/pdbsum/2iy4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iy4 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=2iy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iy4 OCA], [https://pdbe.org/2iy4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iy4 RCSB], [https://www.ebi.ac.uk/pdbsum/2iy4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iy4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DPS_LISMO DPS_LISMO]] Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction. Does not bind to DNA (By similarity). Dps is important for full resistance to heat and cold shocks and is essential for full virulence of this bacterium. It seems to play a direct or indirect role on the production and/or stability of listeriolysin O.<ref>PMID:12383509</ref> <ref>PMID:15758237</ref> <ref>PMID:16098690</ref>
+[[https://www.uniprot.org/uniprot/DPS_LISMO DPS_LISMO]] Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction. Does not bind to DNA (By similarity). Dps is important for full resistance to heat and cold shocks and is essential for full virulence of this bacterium. It seems to play a direct or indirect role on the production and/or stability of listeriolysin O.<ref>PMID:12383509</ref> <ref>PMID:15758237</ref> <ref>PMID:16098690</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2iy4

From Proteopedia

Revision as of 07:56, 19 January 2022

X-ray structure of Dps from Listeria monocytogenes

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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