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1thx

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[[Image:1thx.jpg|left|200px]]
 
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{{Structure
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==THIOREDOXIN-2==
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|PDB= 1thx |SIZE=350|CAPTION= <scene name='initialview01'>1thx</scene>, resolution 1.6&Aring;
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<StructureSection load='1thx' size='340' side='right'caption='[[1thx]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1thx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1THX FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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|GENE= TRXA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1167 Anabaena sp.])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1thx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1thx OCA], [https://pdbe.org/1thx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1thx RCSB], [https://www.ebi.ac.uk/pdbsum/1thx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1thx ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1thx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1thx OCA], [http://www.ebi.ac.uk/pdbsum/1thx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1thx RCSB]</span>
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[https://www.uniprot.org/uniprot/THIO2_NOSS1 THIO2_NOSS1] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/th/1thx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1thx ConSurf].
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<div style="clear:both"></div>
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'''THIOREDOXIN-2'''
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==See Also==
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*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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BACKGROUND: Thioredoxins are ubiquitous proteins that serve as reducing agents and general protein disulfide reductases. The structures of thioredoxins from a number of species, including man and Escherichia coli, are known. Cyanobacteria, such as Anabaena, contain two thioredoxins that exhibit very different activities with target enzymes and share little sequence similarity. Thioredoxin-2 (Trx-2) from Anabaena resembles chloroplast type-f thioredoxin in its activities and the two proteins may be evolutionarily related. We have undertaken structural studies of Trx-2 in order to gain insights into the structure/function relationships of thioredoxins. RESULTS: Anabaena Trx-2, like E. coli thioredoxin, consists of a five-stranded beta sheet core surrounded by four alpha helices. The active site includes a conserved disulfide ring (in the sequence 31WCGPC35). An aspartate (E. coli) to tyrosine (Trx-2) substitution alters the position of this disulfide ring relative to the central pleated sheet. However, loss of this conserved aspartate does not affect the disulfide geometry. In the Trx-2 crystals, the N-terminal residues make extensive contacts with a symmetry-related molecule with hydrogen bonds to residues 74-76 mimicking thioredoxin-protein interactions. CONCLUSIONS: The overall three-dimensional structure of Trx-2 is similar to E. coli thioredoxin and other related disulfide oxido-reductases. Single amino acid substitutions around the protein interaction area probably account for the unusual enzymatic activities of Trx-2 and its ability to discriminate between substrate and non-substrate peptides.
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[[Category: Large Structures]]
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[[Category: Nostoc sp. PCC 7120 = FACHB-418]]
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==About this Structure==
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[[Category: Eklund H]]
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1THX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THX OCA].
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[[Category: Gleason FK]]
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[[Category: Saarinen M]]
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==Reference==
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Crystal structure of thioredoxin-2 from Anabaena., Saarinen M, Gleason FK, Eklund H, Structure. 1995 Oct 15;3(10):1097-108. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8590004 8590004]
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[[Category: Anabaena sp.]]
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[[Category: Single protein]]
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[[Category: Eklund, H.]]
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[[Category: Gleason, F K.]]
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[[Category: Saarinen, M.]]
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[[Category: oxido-reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:56:15 2008''
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Current revision

THIOREDOXIN-2

PDB ID 1thx

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