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| | <StructureSection load='4aj8' size='340' side='right'caption='[[4aj8]], [[Resolution|resolution]] 1.54Å' scene=''> | | <StructureSection load='4aj8' size='340' side='right'caption='[[4aj8]], [[Resolution|resolution]] 1.54Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4aj8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Litopenaeus_vannamei Litopenaeus vannamei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AJ8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AJ8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4aj8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Penaeus_vannamei Penaeus vannamei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AJ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AJ8 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.54Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zzx|3zzx]], [[4aj6|4aj6]], [[4aj7|4aj7]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4aj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aj8 OCA], [https://pdbe.org/4aj8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aj8 RCSB], [https://www.ebi.ac.uk/pdbsum/4aj8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aj8 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=4aj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aj8 OCA], [http://pdbe.org/4aj8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4aj8 RCSB], [http://www.ebi.ac.uk/pdbsum/4aj8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4aj8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B1PWB9_PENVA B1PWB9_PENVA] |
| | <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== |
| - | *[[Thioredoxin|Thioredoxin]] | + | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Litopenaeus vannamei]] | + | [[Category: Large Structures]] |
| - | [[Category: Thioredoxin-disulfide reductase]] | + | [[Category: Penaeus vannamei]] |
| - | [[Category: Campos-Acevedo, A A]] | + | [[Category: Campos-Acevedo AA]] |
| - | [[Category: Rudino-Pinera, E]] | + | [[Category: Rudino-Pinera E]] |
| - | [[Category: Sotelo-Mundo, R R]] | + | [[Category: Sotelo-Mundo RR]] |
| - | [[Category: Disulfide reduction]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
B1PWB9_PENVA
Publication Abstract from PubMed
Thioredoxin (Trx) is a 12 kDa cellular redox protein that belongs to a family of small redox proteins which undergo reversible oxidation to produce a cystine disulfide bond through the transfer of reducing equivalents from the catalytic site cysteine residues (Cys32 and Cys35) to a disulfide substrate. In this study, crystals of thioredoxin 1 from the Pacific whiteleg shrimp Litopenaeus vannamei (LvTrx) were successfully obtained. One data set was collected from each of four crystals at 100 K and the three-dimensional structures of the catalytic cysteines in different redox states were determined: reduced and oxidized forms at 2.00 A resolution using data collected at a synchrotron-radiation source and two partially reduced structures at 1.54 and 1.88 A resolution using data collected using an in-house source. All of the crystals belonged to space group P3212, with unit-cell parameters a = 57.5 (4), b = 57.5 (4), c = 118.1 (8) A. The asymmetric unit contains two subunits of LvTrx, with a Matthews coefficient (VM) of 2.31 A(3) Da(-1) and a solvent content of 46%. Initial phases were determined by molecular replacement using the crystallographic model of Trx from Drosophila melanogaster as a template. In the present work, LvTrx was overexpressed in Escherichia coli, purified and crystallized. Structural analysis of the different redox states at the Trx active site highlights its reactivity and corroborates the existence of a dimer in the crystal. In the crystallographic structures the dimer is stabilized by several interactions, including a disulfide bridge between Cys73 of each LvTrx monomer, a hydrogen bond between the side chain of Asp60 of each monomer and several hydrophobic interactions, with a noncrystallographic twofold axis.
Expression, purification, crystallization and X-ray crystallographic studies of different redox states of the active site of thioredoxin 1 from the whiteleg shrimp Litopenaeus vannamei.,Campos-Acevedo AA, Garcia-Orozco KD, Sotelo-Mundo RR, Rudino-Pinera E Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May;69(Pt 5):488-93. doi: , 10.1107/S1744309113010622. Epub 2013 Apr 27. PMID:23695560[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Campos-Acevedo AA, Garcia-Orozco KD, Sotelo-Mundo RR, Rudino-Pinera E. Expression, purification, crystallization and X-ray crystallographic studies of different redox states of the active site of thioredoxin 1 from the whiteleg shrimp Litopenaeus vannamei. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May;69(Pt 5):488-93. doi: , 10.1107/S1744309113010622. Epub 2013 Apr 27. PMID:23695560 doi:10.1107/S1744309113010622
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