7bz6
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7bz6 is ON HOLD Authors: Chong, S.M.S., Neelagandan, K., Gruber, G. Description: Mycobacterium bovis AhpC Category: Unreleased Structures [[Cat...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Mycobacterium bovis AhpC== | |
| + | <StructureSection load='7bz6' size='340' side='right'caption='[[7bz6]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7bz6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_variant_bovis Mycobacterium tuberculosis variant bovis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BZ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BZ6 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]] 3.302Å</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=7bz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bz6 OCA], [https://pdbe.org/7bz6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bz6 RCSB], [https://www.ebi.ac.uk/pdbsum/7bz6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bz6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q79CV0_MYCBI Q79CV0_MYCBI] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The ability of Mycobacteria to overcome oxidative stress is of paramount importance for its survival within the host. One of the key enzymes that are involved in protecting the bacterium from reactive oxygen species is the catalase-peroxidase (KatG). However, in strains resistant to the antibiotic isoniazid, KatG is rendered ineffective, which is associated with an increased expression of alkylhydroperoxide reductase subunit C (AhpC). Mycobacterial AhpC possesses a unique helical displacement when compared to its bacterial counterparts. Here, via mutagenesis studies, we demonstrate the importance of this helix for redox modulation of the catalytic activity of AhpC. Along with structural insights from crystallographic data, the impact of critical residues on the structure and flexibility of the helix and on AhpC oligomerization is described. | ||
| - | + | Residues of helix a2 are critical for catalytic efficiency of mycobacterial alkylhydroperoxide reductase subunit C.,Chong SMS, Kamariah N, Gruber G FEBS Lett. 2020 Sep;594(17):2829-2839. doi: 10.1002/1873-3468.13864. Epub 2020, Jul 20. PMID:32557576<ref>PMID:32557576</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7bz6" style="background-color:#fffaf0;"></div> |
| - | [[Category: Chong | + | == References == |
| - | [[Category: Neelagandan | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mycobacterium tuberculosis variant bovis]] | ||
| + | [[Category: Chong SMS]] | ||
| + | [[Category: Gruber G]] | ||
| + | [[Category: Neelagandan K]] | ||
Current revision
Mycobacterium bovis AhpC
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