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| | ==Wild type Salmonella Alkyl Hydroperoxide Reductase C in its substrate-ready conformation== | | ==Wild type Salmonella Alkyl Hydroperoxide Reductase C in its substrate-ready conformation== |
| - | <StructureSection load='4ma9' size='340' side='right' caption='[[4ma9]], [[Resolution|resolution]] 1.82Å' scene=''> | + | <StructureSection load='4ma9' size='340' side='right'caption='[[4ma9]], [[Resolution|resolution]] 1.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ma9]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MA9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MA9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ma9]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MA9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1n8j|1n8j]], [[1yep|1yep]], [[4mab|4mab]]</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=4ma9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ma9 OCA], [https://pdbe.org/4ma9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ma9 RCSB], [https://www.ebi.ac.uk/pdbsum/4ma9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ma9 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ahpC, ahpC STM0608, STM0608 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</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=4ma9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ma9 OCA], [http://pdbe.org/4ma9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ma9 RCSB], [http://www.ebi.ac.uk/pdbsum/4ma9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ma9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AHPC_SALTY AHPC_SALTY]] Directly reduces alkyl hydroperoxides with the use of electrons donated by the 57 kDa flavoprotein alkyl hydroperoxide reductase. | + | [https://www.uniprot.org/uniprot/AHPC_SALTY AHPC_SALTY] Directly reduces alkyl hydroperoxides with the use of electrons donated by the 57 kDa flavoprotein alkyl hydroperoxide reductase. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus typhimurium loeffler 1892]] | + | [[Category: Large Structures]] |
| - | [[Category: Peroxiredoxin]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] |
| - | [[Category: Karplus, P A]] | + | [[Category: Karplus PA]] |
| - | [[Category: Perkins, A]] | + | [[Category: Perkins A]] |
| - | [[Category: 2-cys prx]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxidase]]
| + | |
| - | [[Category: Prx1 ahpc]]
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| - | [[Category: Thioredoxin fold]]
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| Structural highlights
Function
AHPC_SALTY Directly reduces alkyl hydroperoxides with the use of electrons donated by the 57 kDa flavoprotein alkyl hydroperoxide reductase.
Publication Abstract from PubMed
The catalytic activity of peroxiredoxins (Prx), the dominant peroxidases in most organisms, requires a key cysteine in a substrate-ready fully folded (FF) conformation. This peroxidatic Cys is oxidized to sulfenic acid by the peroxide substrate, and then further reacts, after a local unfolding of the active site, to form a disulfide bond with a second 'resolving' Cys. For Salmonella typhimurium alkyl hydroperoxide reductase C (StAhpC) and some other Prxs, the FF structure is only known for an active site Cys-->Ser variant, and it is assumed that this variant accurately represents the wild type enzyme. Here, we have been able to determine the structure of authentic reduced wild type StAhpC by dithiothreitol treatment of crystals of a previously-solved disulfide form of the wild type enzyme. Structural comparisons allow us to define small, but real shifts in the active site and alterations to the dynamic properties that are caused by the Ser-mutation. We further characterize a linkage between the folding of the active site loop and C-terminal region and use this information to develop a strategy to crystallize the C165A variant (with the resolving Cys mutated to Ala) in the same crystal form. These data reveal how subtle modifications to Prx structures can substantially influence the enzymatic properties and that caution should be exercised in inferring wild type enzyme properties from the behavior of peroxidatic or resolving Cys mutants. We present a simple thermodynamic framework for rationalizing these impacts as well as those of physiologically-relevant regulatory posttranslational modifications and also propose a non-traditional strategy for designing selective Prx inhibitors.
Substrate-ready Conformation of Wild Type Salmonella typhimurium AhpC and the Sensitive Balance between Fully Folded and Locally Unfolded Conformations.,Perkins A, Nelson KJ, Williams JR, Parsonage D, Poole LB, Karplus PA Biochemistry. 2013 Oct 31. PMID:24175952[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Perkins A, Nelson KJ, Williams JR, Parsonage D, Poole LB, Karplus PA. Substrate-ready Conformation of Wild Type Salmonella typhimurium AhpC and the Sensitive Balance between Fully Folded and Locally Unfolded Conformations. Biochemistry. 2013 Oct 31. PMID:24175952 doi:http://dx.doi.org/10.1021/bi4011573
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