4kw6: Difference between revisions
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==Crystal structure of Peroxiredoxin-1 (C-terminal truncation mutant) from the human hookworm Ancylostoma ceylanicum bound to conoidin A== | ==Crystal structure of Peroxiredoxin-1 (C-terminal truncation mutant) from the human hookworm Ancylostoma ceylanicum bound to conoidin A== | ||
<StructureSection load='4kw6' size='340' side='right' caption='[[4kw6]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='4kw6' size='340' side='right' caption='[[4kw6]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fh8|4fh8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fh8|4fh8]]</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='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=4kw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kw6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kw6 RCSB], [http://www.ebi.ac.uk/pdbsum/4kw6 PDBsum]</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=4kw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kw6 OCA], [http://pdbe.org/4kw6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kw6 RCSB], [http://www.ebi.ac.uk/pdbsum/4kw6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kw6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4kw6" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 11:08, 5 August 2016
Crystal structure of Peroxiredoxin-1 (C-terminal truncation mutant) from the human hookworm Ancylostoma ceylanicum bound to conoidin ACrystal structure of Peroxiredoxin-1 (C-terminal truncation mutant) from the human hookworm Ancylostoma ceylanicum bound to conoidin A
Structural highlights
Publication Abstract from PubMedHookworms are parasitic nematodes that have a devastating impact on global health, particularly in developing countries. We report a biochemical and structural analysis of a peroxiredoxin from the hookworm Ancylostoma ceylanicum, AcePrx-1. Peroxiredoxins provide antioxidant protection and act as signaling molecules and chaperones. AcePrx-1 is expressed in adult hookworms and can be inactivated by 2,3-bis(bromomethyl)quinoxaline-1,4-dioxide (conoidin A). Conoidin A inactivates AcePrx-1 by alkylating or crosslinking the catalytic cysteines, while maintaining the enzyme in the "locally unfolded" conformation. Irreversible oxidation of the resolving cysteine may contribute additional inhibitory activity. A crystal structure of oxidized AcePrx-1 reveals a disulfide-linked decamer. A helix macrodipole near the active site increases the reactivity of the catalytic cysteines to conoidin A. This work demonstrates the promise of conoidin compounds as probes to evaluate peroxiredoxins as drug targets in human parasites. Peroxiredoxin-1 from the Human Hookworm Ancylostoma ceylanicum Forms a Stable Oxidized Decamer and Is Covalently Inhibited by Conoidin A.,Nguyen JB, Pool CD, Wong CY, Treger RS, Williams DL, Cappello M, Lea WA, Simeonov A, Vermeire JJ, Modis Y Chem Biol. 2013 Jul 23. pii: S1074-5521(13)00244-5. doi:, 10.1016/j.chembiol.2013.06.011. PMID:23891152[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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