4oo5
From Proteopedia
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- | + | ==Crystal Structure of S-nitrosated Human Thioredoxin Mutant== | |
- | + | <StructureSection load='4oo5' size='340' side='right' caption='[[4oo5]], [[Resolution|resolution]] 1.54Å' scene=''> | |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[4oo5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OO5 FirstGlance]. <br> | ||
+ | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SNC:S-NITROSO-CYSTEINE'>SNC</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3m9j|3m9j]], [[3m9k|3m9k]], [[2iiy|2iiy]], [[2hxk|2hxk]], [[4oo4|4oo4]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TXN, TRDX, TRX, TRX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4oo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oo5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oo5 RCSB], [http://www.ebi.ac.uk/pdbsum/4oo5 PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Thioredoxins reduce disulfide bonds and other thiol modifications in all cells, using a CXXC motif. Human thioredoxin 1 is unusual in that it codes for an additional three cysteines in its 105 amino acid sequence, each of which have been implicated in other reductive activities. Cys 62 and Cys 69 are buried in the protein interior and lie at either end of a short helix (helix 3), and yet can disulfide link under oxidizing conditions. Cys 62 is readily S-nitrosated, giving rise to a SNO modification, which is also buried. Here, we present two crystal structures of the C69S/C73S mutant protein under oxidizing (1.5 A) and reducing (1.1 A) conditions. In the oxidized structure, helix 3 is unraveled and displays a new conformation that is stabilized by a series of new hydrogen bonds and a disulfide link with Cys 62 in a neighboring molecule. The new conformation provides an explanation for how a completely buried residue can participate in SNO exchange reactions. | ||
- | + | Crystal structure of human thioredoxin revealing an unraveled helix and exposed S- nitrosation site.,Weichsel A, Kem M, Montfort WR Protein Sci. 2010 Jul 26. PMID:20662007<ref>PMID:20662007</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | == | + | ==See Also== |
- | + | *[[Thioredoxin|Thioredoxin]] | |
- | [[Category: Montfort, W R | + | == References == |
- | [[Category: The, J | + | <references/> |
- | [[Category: Weichsel, A | + | __TOC__ |
+ | </StructureSection> | ||
+ | [[Category: Human]] | ||
+ | [[Category: Montfort, W R]] | ||
+ | [[Category: The, J]] | ||
+ | [[Category: Weichsel, A]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: S-nitrosation]] | [[Category: S-nitrosation]] | ||
[[Category: S-nitrosocysteine]] | [[Category: S-nitrosocysteine]] |
Revision as of 04:40, 22 December 2014
Crystal Structure of S-nitrosated Human Thioredoxin Mutant
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