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| | <StructureSection load='5ovq' size='340' side='right'caption='[[5ovq]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='5ovq' size='340' side='right'caption='[[5ovq]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ovq]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus_(strain_vf5) Aquifex aeolicus (strain vf5)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OVQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5OVQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ovq]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OVQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</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]] 1.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peroxiredoxin Peroxiredoxin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.15 1.11.1.15] </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=5ovq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ovq OCA], [https://pdbe.org/5ovq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ovq RCSB], [https://www.ebi.ac.uk/pdbsum/5ovq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ovq ProSAT]</span></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=5ovq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ovq OCA], [http://pdbe.org/5ovq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ovq RCSB], [http://www.ebi.ac.uk/pdbsum/5ovq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ovq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TDXH_AQUAE TDXH_AQUAE]] Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. | + | [https://www.uniprot.org/uniprot/TDXH_AQUAE TDXH_AQUAE] Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Aquifex aeolicus VF5]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peroxiredoxin]]
| + | [[Category: Peng G]] |
| - | [[Category: Peng, G]] | + | [[Category: Warkentin E]] |
| - | [[Category: Warkentin, E]] | + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
TDXH_AQUAE Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Publication Abstract from PubMed
Peroxiredoxins (Prxs) are thiol peroxidases that scavenge various peroxide substrates such as hydrogen peroxide (H2O2), alkyl hydroperoxides and peroxinitrite. They also function as chaperones and are involved in signal transduction by H2O2 in eukaryotic cells. The genome of Aquifex aeolicus, a microaerophilic, hyperthermophilic eubacterium, encodes four Prxs, among them an alkyl hydroperoxide reductase AhpC2 which was found to be closely related to archaeal 1-Cys peroxiredoxins. We determined the crystal structure of AhpC2 at 1.8A resolution and investigated its oligomeric state in solution by electron microscopy. AhpC2 is arranged as a toroid-shaped dodecamer instead of the typically observed decamer. The basic folding topology and the active site structure are conserved and possess a high structural similarity to other 1-Cys Prxs. However, the C-terminal region adopts an opposite orientation. AhpC2 contains three cysteines, Cys(49), Cys(212), and Cys(218). The peroxidatic cysteine CP(49) was found to be hyperoxidized to the sulfonic acid (SO3H) form, while Cys(212) forms an intra-monomer disulfide bond with Cys(218). Mutagenesis experiments indicate that Cys(212) and Cys(218) play important roles in the oligomerization of AhpC2. Based on these structural characteristics, we proposed the catalytic mechanism of AhpC2. This study provides novel insights into the structure and reaction mechanism of 1-Cys peroxiredoxins.
Structural properties of the peroxiredoxin AhpC2 from the hyperthermophilic eubacterium Aquifex aeolicus.,Liu W, Liu A, Gao H, Wang Q, Wang L, Warkentin E, Rao Z, Michel H, Peng G Biochim Biophys Acta Gen Subj. 2018 Aug 24;1862(12):2797-2805. doi:, 10.1016/j.bbagen.2018.08.017. PMID:30251668[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu W, Liu A, Gao H, Wang Q, Wang L, Warkentin E, Rao Z, Michel H, Peng G. Structural properties of the peroxiredoxin AhpC2 from the hyperthermophilic eubacterium Aquifex aeolicus. Biochim Biophys Acta Gen Subj. 2018 Aug 24;1862(12):2797-2805. doi:, 10.1016/j.bbagen.2018.08.017. PMID:30251668 doi:http://dx.doi.org/10.1016/j.bbagen.2018.08.017
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