1ti3
From Proteopedia
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| - | [[Image:1ti3.gif|left|200px]]<br /><applet load="1ti3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1ti3" /> | ||
| - | '''Solution structure of the Thioredoxin h1 from poplar, a CPPC active site variant'''<br /> | ||
| - | == | + | ==Solution structure of the Thioredoxin h1 from poplar, a CPPC active site variant== |
| + | <StructureSection load='1ti3' size='340' side='right'caption='[[1ti3]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1ti3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Populus_tremula Populus tremula]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TI3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1ti3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ti3 OCA], [https://pdbe.org/1ti3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ti3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ti3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ti3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q8S3L3_POPPZ Q8S3L3_POPPZ] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ti/1ti3_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1ti3 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Assignment of heteronuclear and homonuclear multidimensional NMR spectra permits determination of the first three-dimensional solution structure of a higher-plant thioredoxin h. The collection of 1906 distance restraints, 137 TALOS-derived dihedral restraints, and 66 hydrogen bonds was used in the restrained molecular dynamics protocol to calculate the structure of the reduced form of thioredoxin h1 from poplar with an atomic rmsd of 0.60 +/- 0.12 A. This enzyme exhibits an unusual active site with the sequence WCPPC and original properties in terms of stability and specificity. Compared to other known thioredoxin structures, thioredoxin h1 from poplar adopts the classical "Trx fold". Its atypical active site possesses a conformation similar to that of other common thioredoxins but appears to be more rigid. Moreover, the hydrogen bond network, stabilizing the in-core beta-sheet, is tighter than in Chlamydomonas reinhardtii, explaining the difference in thermostability. | Assignment of heteronuclear and homonuclear multidimensional NMR spectra permits determination of the first three-dimensional solution structure of a higher-plant thioredoxin h. The collection of 1906 distance restraints, 137 TALOS-derived dihedral restraints, and 66 hydrogen bonds was used in the restrained molecular dynamics protocol to calculate the structure of the reduced form of thioredoxin h1 from poplar with an atomic rmsd of 0.60 +/- 0.12 A. This enzyme exhibits an unusual active site with the sequence WCPPC and original properties in terms of stability and specificity. Compared to other known thioredoxin structures, thioredoxin h1 from poplar adopts the classical "Trx fold". Its atypical active site possesses a conformation similar to that of other common thioredoxins but appears to be more rigid. Moreover, the hydrogen bond network, stabilizing the in-core beta-sheet, is tighter than in Chlamydomonas reinhardtii, explaining the difference in thermostability. | ||
| - | + | Solution structure of a natural CPPC active site variant, the reduced form of thioredoxin h1 from poplar.,Coudevylle N, Thureau A, Hemmerlin C, Gelhaye E, Jacquot JP, Cung MT Biochemistry. 2005 Feb 15;44(6):2001-8. PMID:15697225<ref>PMID:15697225</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1ti3" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Populus tremula]] | ||
| + | [[Category: Coudevylle N]] | ||
| + | [[Category: Cung MT]] | ||
| + | [[Category: Gelhaye E]] | ||
| + | [[Category: Hemmerlin C]] | ||
| + | [[Category: Jacquot JP]] | ||
| + | [[Category: Thureau A]] | ||
Current revision
Solution structure of the Thioredoxin h1 from poplar, a CPPC active site variant
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