2iwt: Difference between revisions
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==Thioredoxin h2 (HvTrxh2) in a mixed disulfide complex with the target protein BASI== | ==Thioredoxin h2 (HvTrxh2) in a mixed disulfide complex with the target protein BASI== | ||
<StructureSection load='2iwt' size='340' side='right' caption='[[2iwt]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2iwt' size='340' side='right'caption='[[2iwt]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2iwt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Barley Barley]. 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 [http:// | <table><tr><td colspan='2'>[[2iwt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Barley Barley]. 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 [http://proteopedia.org/fgij/fg.htm?mol=2IWT FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr> | </td></tr><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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ava|1ava]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ava|1ava]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2iwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwt OCA], [http://pdbe.org/2iwt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iwt RCSB], [http://www.ebi.ac.uk/pdbsum/2iwt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iwt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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==See Also== | ==See Also== | ||
*[[Thioredoxin|Thioredoxin]] | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Barley]] | [[Category: Barley]] | ||
[[Category: Large Structures]] | |||
[[Category: Finnie, C]] | [[Category: Finnie, C]] | ||
[[Category: Hagglund, P]] | [[Category: Hagglund, P]] | ||
Revision as of 10:33, 15 April 2020
Thioredoxin h2 (HvTrxh2) in a mixed disulfide complex with the target protein BASIThioredoxin h2 (HvTrxh2) in a mixed disulfide complex with the target protein BASI
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThioredoxin 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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