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3a5w
From Proteopedia
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| - | [[Image:3a5w.png|left|200px]] | ||
| - | + | ==Peroxiredoxin (wild type) from Aeropyrum pernix K1 (reduced form)== | |
| + | <StructureSection load='3a5w' size='340' side='right'caption='[[3a5w]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3a5w]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Aerpe Aerpe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A5W FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3a2v|3a2v]], [[3a2w|3a2w]], [[3a2x|3a2x]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APE_2278 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272557 AERPE])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peroxiredoxin Peroxiredoxin], with EC number [https://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=3a5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a5w OCA], [https://pdbe.org/3a5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a5w RCSB], [https://www.ebi.ac.uk/pdbsum/3a5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a5w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a5/3a5w_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3a5w ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Peroxiredoxin (Prx) reduces hydrogen peroxide and alkyl peroxides to water and corresponding alcohols, respectively. The reaction is dependent on a peroxidatic cysteine, whose sulphur atom nucleophilically attacks one of the oxygen atoms of the peroxide substrate. In spite of the many structural studies that have been carried out on this reaction, the tertiary structure of the hydrogen peroxide-bound form of Prx has not been elucidated. In this paper, we report the crystal structure of Prx from Aeropyrum pernix K1 in the peroxide-bound form. The conformation of the polypeptide chain is the same as that in the reduced apo-form. The hydrogen peroxide molecule is in close contact with the peroxidatic Cys50 and the neighbouring Thr47 and Arg126 side chain atoms, as well as with the main chain nitrogen atoms of Val49 and Cys50. Bound peroxide was also observed in the mutant C50S, in which the peroxidatic cysteine was replaced by serine. Therefore, the sulphur atom of the peroxidatic cysteine is not essential for peroxide binding, although it enhances the binding affinity. Hydrogen peroxide binds to the protein so that it fills the active site pocket. This study provides insight into the early stage of the Prx reaction. | ||
| - | + | Crystal structure of peroxiredoxin from Aeropyrum pernix K1 complexed with its substrate, hydrogen peroxide.,Nakamura T, Kado Y, Yamaguchi T, Matsumura H, Ishikawa K, Inoue T J Biochem. 2010 Jan;147(1):109-15. Epub 2009 Oct 9. PMID:19819903<ref>PMID:19819903</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3a5w" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | < | + | </StructureSection> |
| - | [[Category: | + | [[Category: Aerpe]] |
| + | [[Category: Large Structures]] | ||
[[Category: Peroxiredoxin]] | [[Category: Peroxiredoxin]] | ||
| - | [[Category: Inoue, T | + | [[Category: Inoue, T]] |
| - | [[Category: Ishikawa, K | + | [[Category: Ishikawa, K]] |
| - | [[Category: Kado, Y | + | [[Category: Kado, Y]] |
| - | [[Category: Matsumura, H | + | [[Category: Matsumura, H]] |
| - | [[Category: Nakamura, T | + | [[Category: Nakamura, T]] |
| - | [[Category: Yamaguchi, T | + | [[Category: Yamaguchi, T]] |
[[Category: Antioxidant]] | [[Category: Antioxidant]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
| - | [[Category: Peroxiredoxin]] | ||
[[Category: Redox-active center]] | [[Category: Redox-active center]] | ||
[[Category: Thioredoxin peroxidase]] | [[Category: Thioredoxin peroxidase]] | ||
Current revision
Peroxiredoxin (wild type) from Aeropyrum pernix K1 (reduced form)
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