5zte
From Proteopedia
(Difference between revisions)
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| - | ==Crystal structure of | + | ==Crystal structure of PrxA C119S mutant from Arabidopsis thaliana== |
<StructureSection load='5zte' size='340' side='right' caption='[[5zte]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='5zte' size='340' side='right' caption='[[5zte]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5zte]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZTE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZTE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zte]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZTE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZTE FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAS1, At3g11630, F24K9.28, T19F11.3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=5zte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zte OCA], [http://pdbe.org/5zte PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zte RCSB], [http://www.ebi.ac.uk/pdbsum/5zte PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zte ProSAT]</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=5zte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zte OCA], [http://pdbe.org/5zte PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zte RCSB], [http://www.ebi.ac.uk/pdbsum/5zte PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zte ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/BAS1A_ARATH BAS1A_ARATH]] Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. May be an antioxidant enzyme particularly in the developing shoot and photosynthesizing leaf.<ref>PMID:12084836</ref> | [[http://www.uniprot.org/uniprot/BAS1A_ARATH BAS1A_ARATH]] Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. May be an antioxidant enzyme particularly in the developing shoot and photosynthesizing leaf.<ref>PMID:12084836</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Peroxiredoxins (Prxs), a large family of antioxidant enzymes, are abundant in all living organisms. Peroxiredoxin A (PrxA) from Arabidopsis thaliana belongs to the typical 2-Cys Prx family and is localized in the chloroplast. This article reports the crystal structure of a PrxA C119S mutant refined to 2.6 A resolution. The protein exists as a decamer both in the crystal structure and in solution. The structure is in the reduced state suitable for the approach of peroxide, though conformational changes are needed for the resolving process. | ||
| + | |||
| + | Crystal structure of Arabidopsis thaliana peroxiredoxin A C119S mutant.,Yang Y, Cai W, Wang J, Pan W, Liu L, Wang M, Zhang M Acta Crystallogr F Struct Biol Commun. 2018 Oct 1;74(Pt 10):625-631. doi:, 10.1107/S2053230X18010920. Epub 2018 Sep 19. PMID:30279313<ref>PMID:30279313</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5zte" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Arath]] | ||
[[Category: Peroxiredoxin]] | [[Category: Peroxiredoxin]] | ||
[[Category: Cai, W]] | [[Category: Cai, W]] | ||
Revision as of 06:37, 24 October 2018
Crystal structure of PrxA C119S mutant from Arabidopsis thaliana
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