2iwt

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[[Image:2iwt.jpg|left|200px]]
 
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{{Structure
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==Thioredoxin h2 (HvTrxh2) in a mixed disulfide complex with the target protein BASI==
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|PDB= 2iwt |SIZE=350|CAPTION= <scene name='initialview01'>2iwt</scene>, resolution 2.30&Aring;
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<StructureSection load='2iwt' size='340' side='right'caption='[[2iwt]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Flc+Binding+Site+For+Chain+B'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>
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<table><tr><td colspan='2'>[[2iwt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IWT 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]] 2.3&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr>
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|DOMAIN=
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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=2iwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwt OCA], [https://pdbe.org/2iwt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iwt RCSB], [https://www.ebi.ac.uk/pdbsum/2iwt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iwt ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwt OCA], [http://www.ebi.ac.uk/pdbsum/2iwt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iwt RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/IAAS_HORVU IAAS_HORVU] This protein inhibits independently subtilisin and alpha-amylase.
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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/iw/2iwt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2iwt ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Thioredoxin is ubiquitous and regulates various target proteins through disulfide bond reduction. We report the structure of thioredoxin (HvTrxh2 from barley) in a reaction intermediate complex with a protein substrate, barley alpha-amylase/subtilisin inhibitor (BASI). The crystal structure of this mixed disulfide shows a conserved hydrophobic motif in thioredoxin interacting with a sequence of residues from BASI through van der Waals contacts and backbone-backbone hydrogen bonds. The observed structural complementarity suggests that the recognition of features around protein disulfides plays a major role in the specificity and protein disulfide reductase activity of thioredoxin. This novel insight into the function of thioredoxin constitutes a basis for comprehensive understanding of its biological role. Moreover, comparison with structurally related proteins shows that thioredoxin shares a mechanism with glutaredoxin and glutathione transferase for correctly positioning substrate cysteine residues at the catalytic groups but possesses a unique structural element that allows recognition of protein disulfides.
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'''THIOREDOXIN H2 (HVTRXH2) IN A MIXED DISULFIDE COMPLEX WITH THE TARGET PROTEIN BASI'''
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Structural basis for target protein recognition by the protein disulfide reductase thioredoxin.,Maeda K, Hagglund P, Finnie C, Svensson B, Henriksen A Structure. 2006 Nov;14(11):1701-10. PMID:17098195<ref>PMID:17098195</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2iwt" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Thioredoxin is ubiquitous and regulates various target proteins through disulfide bond reduction. We report the structure of thioredoxin (HvTrxh2 from barley) in a reaction intermediate complex with a protein substrate, barley alpha-amylase/subtilisin inhibitor (BASI). The crystal structure of this mixed disulfide shows a conserved hydrophobic motif in thioredoxin interacting with a sequence of residues from BASI through van der Waals contacts and backbone-backbone hydrogen bonds. The observed structural complementarity suggests that the recognition of features around protein disulfides plays a major role in the specificity and protein disulfide reductase activity of thioredoxin. This novel insight into the function of thioredoxin constitutes a basis for comprehensive understanding of its biological role. Moreover, comparison with structurally related proteins shows that thioredoxin shares a mechanism with glutaredoxin and glutathione transferase for correctly positioning substrate cysteine residues at the catalytic groups but possesses a unique structural element that allows recognition of protein disulfides.
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*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2IWT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IWT OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Structural basis for target protein recognition by the protein disulfide reductase thioredoxin., Maeda K, Hagglund P, Finnie C, Svensson B, Henriksen A, Structure. 2006 Nov;14(11):1701-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17098195 17098195]
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[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Finnie, C.]]
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[[Category: Finnie C]]
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[[Category: Hagglund, P.]]
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[[Category: Hagglund P]]
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[[Category: Henriksen, A.]]
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[[Category: Henriksen A]]
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[[Category: Maeda, K.]]
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[[Category: Maeda K]]
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[[Category: Svensson, B.]]
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[[Category: Svensson B]]
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[[Category: alpha-amylase inhibitor]]
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[[Category: amy2]]
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[[Category: basi]]
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[[Category: disulfide intermediate]]
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[[Category: disulfide reductase]]
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[[Category: oxidoreductase]]
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[[Category: protease inhibitor]]
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[[Category: redox]]
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[[Category: serine protease inhibitor]]
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[[Category: substrate recognition]]
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[[Category: thioredoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:49:46 2008''
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Current revision

Thioredoxin h2 (HvTrxh2) in a mixed disulfide complex with the target protein BASI

PDB ID 2iwt

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