4xih: Difference between revisions
New page: '''Unreleased structure''' The entry 4xih is ON HOLD until Paper Publication Authors: Tamu Dufe, V., van Molle, I., Pallo, A., Messens, J. Description: Crystal structure of the R116A m... |
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==Crystal structure of the R116A mutant AhpE from Mycobacterium tuberculosis== | |||
<StructureSection load='4xih' size='340' side='right'caption='[[4xih]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xih]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_CCDC5079 Mycobacterium tuberculosis CCDC5079]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XIH FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</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=4xih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xih OCA], [https://pdbe.org/4xih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xih RCSB], [https://www.ebi.ac.uk/pdbsum/4xih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xih ProSAT]</span></td></tr> | |||
</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;"> | |||
== 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<ref>PMID:27471753</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4xih" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Pallo | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis CCDC5079]] | |||
[[Category: Messens J]] | |||
[[Category: Pallo A]] | |||
[[Category: Tamu Dufe V]] | |||
[[Category: Van Molle I]] | |||
Latest revision as of 13:48, 10 January 2024
Crystal structure of the R116A mutant AhpE from Mycobacterium tuberculosisCrystal structure of the R116A mutant AhpE from Mycobacterium tuberculosis
Structural highlights
FunctionAHPE_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 PubMedPeroxiredoxins 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. References
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