5c04

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:17, 10 January 2024) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
==Crystal structure of the F37H mutant AhpE from Mycobacterium tuberculosis==
==Crystal structure of the F37H mutant AhpE from Mycobacterium tuberculosis==
-
<StructureSection load='5c04' size='340' side='right' caption='[[5c04]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
+
<StructureSection load='5c04' size='340' side='right'caption='[[5c04]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5c04]] is a 2 chain structure. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</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=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='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;">
 +
== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 5c04" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]]
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Peroxiredoxin]]
+
[[Category: Large Structures]]
-
[[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]]

Current revision

Crystal structure of the F37H mutant AhpE from Mycobacterium tuberculosis

PDB ID 5c04

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5c04"
Personal tools