|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2clb' size='340' side='right'caption='[[2clb]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2clb' size='340' side='right'caption='[[2clb]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2clb]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulso Sulso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CLB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2clb]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CLB 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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.4Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2clb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2clb OCA], [https://pdbe.org/2clb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2clb RCSB], [https://www.ebi.ac.uk/pdbsum/2clb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2clb 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=2clb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2clb OCA], [https://pdbe.org/2clb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2clb RCSB], [https://www.ebi.ac.uk/pdbsum/2clb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2clb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/DPS_SULSO DPS_SULSO]] 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 (By similarity). In vitro, it efficiently oxidizes Fe(2+) in the presence of hydrogen peroxide and stores it as a mineral core.<ref>PMID:16024730</ref>
| + | [https://www.uniprot.org/uniprot/DPS_SACS2 DPS_SACS2] 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 (By similarity). In vitro, it efficiently oxidizes Fe(2+) in the presence of hydrogen peroxide and stores it as a mineral core.<ref>PMID:16024730</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 34: |
Line 34: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sulso]] | + | [[Category: Saccharolobus solfataricus P2]] |
| - | [[Category: Benas, P]] | + | [[Category: Benas P]] |
| - | [[Category: Douglas, T]] | + | [[Category: Douglas T]] |
| - | [[Category: Gauss, G H]] | + | [[Category: Gauss GH]] |
| - | [[Category: Lawrence, C M]] | + | [[Category: Lawrence CM]] |
| - | [[Category: Wiedenheft, B]] | + | [[Category: Wiedenheft B]] |
| - | [[Category: Young, M]] | + | [[Category: Young M]] |
| - | [[Category: Archaea]]
| + | |
| - | [[Category: Bacterioferritin]]
| + | |
| - | [[Category: Di-iron carboxylate]]
| + | |
| - | [[Category: Dp]]
| + | |
| - | [[Category: Dps- like]]
| + | |
| - | [[Category: Hydrogen peroxide]]
| + | |
| - | [[Category: Hypothetical protein]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Oxidative stress]]
| + | |
| Structural highlights
Function
DPS_SACS2 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 (By similarity). In vitro, it efficiently oxidizes Fe(2+) in the presence of hydrogen peroxide and stores it as a mineral core.[1]
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 superfamily of ferritin-like proteins has recently expanded to include a phylogenetically distinct class of proteins termed DPS-like (DPSL) proteins. Despite their distinct genetic signatures, members of this subclass share considerable similarity to previously recognized DPS proteins. Like DPS, these proteins are expressed in response to oxidative stress, form dodecameric cage-like particles, preferentially utilize H(2)O(2) in the controlled oxidation of Fe(2+), and possess a short N-terminal extension implicated in stabilizing cellular DNA. Given these extensive similarities, the functional properties responsible for the preservation of the DPSL signature in the genomes of diverse prokaryotes have been unclear. Here, we describe the crystal structure of a DPSL protein from the thermoacidophilic archaeon Sulfolobus solfataricus. Although the overall fold of the polypeptide chain and the oligomeric state of this protein are indistinguishable from those of authentic DPS proteins, several important differences are observed. First, rather than a ferroxidase site at the subunit interface, as is observed in all other DPS proteins, the ferroxidase site in SsDPSL is buried within the four-helix bundle, similar to bacterioferritin. Second, the structure reveals a channel leading from the exterior surface of SsDPSL to the bacterioferritin-like dimetal binding site, possibly allowing divalent cations and/or H(2)O(2) to access the active site. Third, a pair of cysteine residues unique to DPSL proteins is found adjacent to the dimetal binding site juxtaposed between the exterior surface of the protein and the active site channel. The cysteine residues in this thioferritin motif may play a redox active role, possibly serving to recycle iron at the ferroxidase center.
Structure of the DPS-like protein from Sulfolobus solfataricus reveals a bacterioferritin-like dimetal binding site within a DPS-like dodecameric assembly.,Gauss GH, Benas P, Wiedenheft B, Young M, Douglas T, Lawrence CM Biochemistry. 2006 Sep 12;45(36):10815-27. PMID:16953567[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wiedenheft B, Mosolf J, Willits D, Yeager M, Dryden KA, Young M, Douglas T. An archaeal antioxidant: characterization of a Dps-like protein from Sulfolobus solfataricus. Proc Natl Acad Sci U S A. 2005 Jul 26;102(30):10551-6. Epub 2005 Jul 15. PMID:16024730 doi:http://dx.doi.org/10.1073/pnas.0501497102
- ↑ Gauss GH, Benas P, Wiedenheft B, Young M, Douglas T, Lawrence CM. Structure of the DPS-like protein from Sulfolobus solfataricus reveals a bacterioferritin-like dimetal binding site within a DPS-like dodecameric assembly. Biochemistry. 2006 Sep 12;45(36):10815-27. PMID:16953567 doi:10.1021/bi060782u
|
