4v2n
From Proteopedia
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| - | ''' | + | ==Crystallographic structure of thioredoxin from Litopenaeus vannamei: Radiation damage effect at 85 MGy, focused in disulfide bonds== |
| + | <StructureSection load='4v2n' size='340' side='right' caption='[[4v2n]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4v2n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V2N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V2N FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4v2l|4v2l]], [[4v2m|4v2m]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </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=4v2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v2n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v2n RCSB], [http://www.ebi.ac.uk/pdbsum/4v2n PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Thioredoxin (Trx) is a small 12-kDa redox protein that catalyzes the reduction of disulfide bonds in proteins from different biological systems. A recent study of the crystal structure of white leg shrimp thioredoxin 1 from Litopenaeus vannamei (LvTrx) revealed a dimeric form of the protein mediated by a covalent link through a disulfide bond between Cys73 from each monomer. In the present study, X-ray-induced damage in the catalytic and the interface disulfide bond of LvTrx was studied at atomic resolution at different transmission energies of 8% and 27%, 12.8 keV at 100 K in the beamline I-24 at Diamond Light Source. We found that at an absorbed dose of 32 MGy, the X-ray induces the cleavage of the disulfide bond of each catalytic site; however, the interface disulfide bond was cleaved at an X-ray adsorbed dose of 85 MGy; despite being the most solvent-exposed disulfide bond in LvTrx (~50 A2). This result clearly established that the interface disulfide bond is very stable and, therefore, less susceptible to being reduced by X-rays. In fact, these studies open the possibility of the existence in solution of a dimeric LvTrx. | ||
| - | + | Crystallographic Studies Evidencing the High Energy Tolerance to Disrupting the Interface Disulfide Bond of Thioredoxin 1 from White Leg Shrimp Litopenaeus vannamei.,Campos-Acevedo AA, Rudino-Pinera E Molecules. 2014 Dec 15;19(12):21113-26. doi: 10.3390/molecules191221113. PMID:25517346<ref>PMID:25517346</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Campos-Acevedo, A | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Thioredoxin-disulfide reductase]] | ||
| + | [[Category: Campos-Acevedo, A A]] | ||
[[Category: Rudino-Pinera, E]] | [[Category: Rudino-Pinera, E]] | ||
| + | [[Category: Disulfide bond]] | ||
| + | [[Category: Litopenaeus vannamei]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 13:28, 14 January 2015
Crystallographic structure of thioredoxin from Litopenaeus vannamei: Radiation damage effect at 85 MGy, focused in disulfide bonds
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