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2whd

From Proteopedia

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{{Seed}}
 
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[[Image:2whd.jpg|left|200px]]
 
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<!--
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==Barley NADPH-dependent thioredoxin reductase 2==
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The line below this paragraph, containing "STRUCTURE_2whd", creates the "Structure Box" on the page.
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<StructureSection load='2whd' size='340' side='right'caption='[[2whd]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2whd]] 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=2WHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WHD FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr>
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{{STRUCTURE_2whd| PDB=2whd | SCENE= }}
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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=2whd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2whd OCA], [https://pdbe.org/2whd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2whd RCSB], [https://www.ebi.ac.uk/pdbsum/2whd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2whd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A9LN30_HORVV A9LN30_HORVV]
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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/wh/2whd_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=2whd 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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Thioredoxins (Trxs) are protein disulfide reductases that regulate the intracellular redox environment and are important for seed germination in plants. Trxs are in turn regulated by NADPH-dependent thioredoxin reductases (NTRs), which provide reducing equivalents to Trx using NADPH to recycle Trxs to the active form. Here, the first crystal structure of a cereal NTR, HvNTR2 from Hordeum vulgare (barley), is presented, which is also the first structure of a monocot plant NTR. The structure was determined at 2.6 A resolution and refined to an R(cryst) of 19.0% and an R(free) of 23.8%. The dimeric protein is structurally similar to the structures of AtNTR-B from Arabidopsis thaliana and other known low-molecular-weight NTRs. However, the relative position of the two NTR cofactor-binding domains, the FAD and the NADPH domains, is not the same. The NADPH domain is rotated by 25 degrees and bent by a 38% closure relative to the FAD domain in comparison with AtNTR-B. The structure may represent an intermediate between the two conformations described previously: the flavin-oxidizing (FO) and the flavin-reducing (FR) conformations. Here, analysis of interdomain contacts as well as phylogenetic studies lead to the proposal of a new reaction scheme in which NTR-Trx interactions mediate the FO to FR transformation.
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===BARLEY NADPH-DEPENDENT THIOREDOXIN REDUCTASE 2===
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Structure of Hordeum vulgare NADPH-dependent thioredoxin reductase 2. Unwinding the reaction mechanism.,Kirkensgaard KG, Hagglund P, Finnie C, Svensson B, Henriksen A Acta Crystallogr D Biol Crystallogr. 2009 Sep;65(Pt 9):932-41. Epub 2009, Aug 14. PMID:19690371<ref>PMID:19690371</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 2whd" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19690371}}, adds the Publication Abstract to the page
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*[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19690371 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19690371}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2WHD is a 2 chains 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=2WHD OCA].
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==Reference==
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<ref group="xtra">PMID:19690371</ref><references group="xtra"/>
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[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
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[[Category: Thioredoxin-disulfide reductase]]
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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: Kirkensgaard, K G.]]
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[[Category: Kirkensgaard KG]]
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[[Category: Svensson, B.]]
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[[Category: Svensson B]]
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[[Category: Disulfide oxidoreductase]]
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[[Category: Flavoprotein]]
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[[Category: Germination]]
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[[Category: Ntr]]
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[[Category: Oxidoreductase]]
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[[Category: Redox regulation]]
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[[Category: Redox-active center]]
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[[Category: Seed development]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Sep 3 15:37:40 2009''
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Current revision

Barley NADPH-dependent thioredoxin reductase 2

PDB ID 2whd

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