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| | <StructureSection load='5c04' size='340' side='right'caption='[[5c04]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='5c04' size='340' side='right'caption='[[5c04]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5c04]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C04 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C04 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c04]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C04 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x0x|4x0x]], [[4x1u|4x1u]], [[4xih|4xih]], [[1xxu|1xxu]], [[1xvw|1xvw]]</td></tr> | + | </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=5c04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c04 OCA], [https://pdbe.org/5c04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c04 RCSB], [https://www.ebi.ac.uk/pdbsum/5c04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c04 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT2298 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5c04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c04 OCA], [http://pdbe.org/5c04 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c04 RCSB], [http://www.ebi.ac.uk/pdbsum/5c04 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c04 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AHPE_MYCTU AHPE_MYCTU] 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. May represent an important antioxidant defense against cytotoxic peroxides, especially peroxynitrite, which can be formed by activated macrophages during infection.<ref>PMID:19737009</ref> <ref>PMID:24379404</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peroxiredoxin]] | |
| - | [[Category: Dufe, V T]] | |
| - | [[Category: Messens, J]] | |
| - | [[Category: Pallo, A]] | |
| - | [[Category: 1-cys peroxiredoxin]] | |
| - | [[Category: Active site mutant]] | |
| | [[Category: Mycobacterium tuberculosis]] | | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Dufe VT]] |
| - | [[Category: Thioredoxin fold]] | + | [[Category: Messens J]] |
| | + | [[Category: Pallo A]] |
| Structural highlights
Function
AHPE_MYCTU 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. May represent an important antioxidant defense against cytotoxic peroxides, especially peroxynitrite, which can be formed by activated macrophages during infection.[1] [2]
Publication Abstract from PubMed
Peroxiredoxins catalyze the reduction of peroxides, a process of vital importance to survive oxidative stress. A nucleophilic cysteine, also known as the peroxidatic cysteine, is responsible for this catalytic process. We used the Mycobacterium tuberculosis alkyl hydroperoxide reductase E (MtAhpE) as a model to investigate the effect of the chemical environment on the specificity of the reaction. Using an integrative structural (R116A - PDB ; F37H - PDB ), kinetic and computational approach, we explain the mutational effects of key residues in its environment. This study shows that the active site residues are specifically oriented to create an environment which selectively favours a reaction with peroxides.
The active site architecture in peroxiredoxins: a case study on Mycobacterium tuberculosis AhpE.,Pedre B, van Bergen LA, Pallo A, Rosado LA, Dufe VT, Molle IV, Wahni K, Erdogan H, Alonso M, Proft F, Messens J Chem Commun (Camb). 2016 Jul 29. PMID:27471753[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hugo M, Turell L, Manta B, Botti H, Monteiro G, Netto LE, Alvarez B, Radi R, Trujillo M. Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: kinetics, acidity constants, and conformational dynamics. Biochemistry. 2009 Oct 13;48(40):9416-26. PMID:19737009 doi:10.1021/bi901221s
- ↑ Hugo M, Van Laer K, Reyes AM, Vertommen D, Messens J, Radi R, Trujillo M. Mycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis. J Biol Chem. 2014 Feb 21;289(8):5228-39. PMID:24379404 doi:10.1074/jbc.M113.510248
- ↑ Pedre B, van Bergen LA, Pallo A, Rosado LA, Dufe VT, Molle IV, Wahni K, Erdogan H, Alonso M, Proft F, Messens J. The active site architecture in peroxiredoxins: a case study on Mycobacterium tuberculosis AhpE. Chem Commun (Camb). 2016 Jul 29. PMID:27471753 doi:http://dx.doi.org/10.1039/c6cc02645a
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