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| | <StructureSection load='6q5v' size='340' side='right'caption='[[6q5v]], [[Resolution|resolution]] 2.75Å' scene=''> | | <StructureSection load='6q5v' size='340' side='right'caption='[[6q5v]], [[Resolution|resolution]] 2.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6q5v]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulir Sulir]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6gww 6gww] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6feu 6feu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q5V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q5V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6q5v]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_islandicus_REY15A Sulfolobus islandicus REY15A]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6gww 6gww] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6feu 6feu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q5V FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SiRe_0346 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=930945 SULIR])</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]] 2.747Å</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=6q5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q5v OCA], [https://pdbe.org/6q5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q5v RCSB], [https://www.ebi.ac.uk/pdbsum/6q5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q5v 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=6q5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q5v OCA], [http://pdbe.org/6q5v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q5v RCSB], [http://www.ebi.ac.uk/pdbsum/6q5v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q5v ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/F0NEA3_SULIR F0NEA3_SULIR]] 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.[HAMAP-Rule:MF_00401] | + | [https://www.uniprot.org/uniprot/F0NEA3_SULIR F0NEA3_SULIR] 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.[HAMAP-Rule:MF_00401] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Peroxiredoxin|Peroxiredoxin]] | + | *[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peroxiredoxin]] | + | [[Category: Sulfolobus islandicus REY15A]] |
| - | [[Category: Sulir]]
| + | [[Category: Maes D]] |
| - | [[Category: Maes, D]] | + | [[Category: Peeters E]] |
| - | [[Category: Molle, I van]]
| + | [[Category: Stroobants S]] |
| - | [[Category: Peeters, E]] | + | [[Category: Van Molle I]] |
| - | [[Category: Stroobants, S]] | + | |
| - | [[Category: Archaea]] | + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Sulfolobus islandicus]]
| + | |
| Structural highlights
Function
F0NEA3_SULIR 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.[HAMAP-Rule:MF_00401]
Publication Abstract from PubMed
Aerobic thermoacidophilic archaea belonging to the genus Sulfolobus harbor peroxiredoxins, thiol-dependent peroxidases that assist in protecting the cells from oxidative damage. Here, the crystal structure of the 1-Cys peroxiredoxin from Sulfolobus islandicus, named 1-Cys SiPrx, is presented. A 2.75 A resolution data set was collected from a crystal belonging to space group P212121, with unit-cell parameters a = 86.8, b = 159.1, c = 189.3 A, alpha = beta = gamma = 90 degrees . The structure was solved by molecular replacement using the homologous Aeropyrum pernix peroxiredoxin (ApPrx) structure as a search model. In the crystal structure, 1-Cys SiPrx assembles into a ring-shaped decamer composed of five homodimers. This quaternary structure corresponds to the oligomeric state of the protein in solution, as observed by size-exclusion chromatography. 1-Cys SiPrx harbors only a single cysteine, which is the peroxidatic cysteine, and lacks both of the cysteines that are highly conserved in the C-terminal arm domain in other archaeal Prx6-subfamily proteins such as ApPrx and that are involved in the association of dimers into higher-molecular-weight decamers and dodecamers. It is thus concluded that the Sulfolobus Prx6-subfamily protein undergoes decamerization independently of arm-domain cysteines.
Structure of the Prx6-subfamily 1-Cys peroxiredoxin from Sulfolobus islandicus.,Stroobants S, Van Molle I, Saidi Q, Jonckheere K, Maes D, Peeters E Acta Crystallogr F Struct Biol Commun. 2019 Jun 1;75(Pt 6):428-434. doi:, 10.1107/S2053230X19006472. Epub 2019 May 13. PMID:31204689[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stroobants S, Van Molle I, Saidi Q, Jonckheere K, Maes D, Peeters E. Structure of the Prx6-subfamily 1-Cys peroxiredoxin from Sulfolobus islandicus. Acta Crystallogr F Struct Biol Commun. 2019 Jun 1;75(Pt 6):428-434. doi:, 10.1107/S2053230X19006472. Epub 2019 May 13. PMID:31204689 doi:http://dx.doi.org/10.1107/S2053230X19006472
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