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| | <StructureSection load='4fh8' size='340' side='right'caption='[[4fh8]], [[Resolution|resolution]] 2.11Å' scene=''> | | <StructureSection load='4fh8' size='340' side='right'caption='[[4fh8]], [[Resolution|resolution]] 2.11Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fh8]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Ancylostoma_ceylanicum Ancylostoma ceylanicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FH8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FH8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fh8]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Ancylostoma_ceylanicum Ancylostoma ceylanicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FH8 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fh9|4fh9]], [[3tjb|3tjb]], [[1qmv|1qmv]]</td></tr> | + | </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=4fh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fh8 OCA], [https://pdbe.org/4fh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fh8 RCSB], [https://www.ebi.ac.uk/pdbsum/4fh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fh8 ProSAT]</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=4fh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fh8 OCA], [http://pdbe.org/4fh8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fh8 RCSB], [http://www.ebi.ac.uk/pdbsum/4fh8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fh8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/J7HJM3_9BILA J7HJM3_9BILA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Peroxiredoxin|Peroxiredoxin]] | + | *[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Ancylostoma ceylanicum]] | | [[Category: Ancylostoma ceylanicum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peroxiredoxin]]
| + | [[Category: Modis Y]] |
| - | [[Category: Modis, Y]] | + | [[Category: Nguyen JB]] |
| - | [[Category: Nguyen, J B]] | + | |
| - | [[Category: 2-cys peroxiredoxin]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
J7HJM3_9BILA
Publication Abstract from PubMed
Hookworms 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 Also
References
- ↑ Nguyen JB, Pool CD, Wong CY, Treger RS, Williams DL, Cappello M, Lea WA, Simeonov A, Vermeire JJ, Modis Y. Peroxiredoxin-1 from the Human Hookworm Ancylostoma ceylanicum Forms a Stable Oxidized Decamer and Is Covalently Inhibited by Conoidin A. Chem Biol. 2013 Jul 23. pii: S1074-5521(13)00244-5. doi:, 10.1016/j.chembiol.2013.06.011. PMID:23891152 doi:10.1016/j.chembiol.2013.06.011
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