1ilo
From Proteopedia
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| - | [[Image:1ilo.gif|left|200px]]<br /><applet load="1ilo" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1ilo" /> | ||
| - | '''NMR structure of a thioredoxin, MtH895, from the archeon Methanobacterium thermoautotrophicum strain delta H.'''<br /> | ||
| - | == | + | ==NMR structure of a thioredoxin, MtH895, from the archeon Methanobacterium thermoautotrophicum strain delta H.== |
| + | <StructureSection load='1ilo' size='340' side='right'caption='[[1ilo]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1ilo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus_str._Delta_H Methanothermobacter thermautotrophicus str. Delta H]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ILO 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=1ilo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ilo OCA], [https://pdbe.org/1ilo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ilo RCSB], [https://www.ebi.ac.uk/pdbsum/1ilo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ilo ProSAT], [https://www.topsan.org/Proteins/NESGC/1ilo TOPSAN]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/THIRX_METTH THIRX_METTH] Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase. Has low thioredoxin activity in vitro.<ref>PMID:11939770</ref> | ||
| + | == 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/il/1ilo_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=1ilo ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
As part of a high-throughput, structural proteomic project we have used NMR spectroscopy to determine the solution structure and ascertain the function of a previously unknown, conserved protein (MtH895) from the thermophilic archeon Methanobacterium thermoautotrophicum. Our findings indicate that MtH895 contains a central four-stranded beta-sheet core surrounded by two helices on one side and a third on the other. It has an overall fold superficially similar to that of a glutaredoxin. However, detailed analysis of its three-dimensional structure along with molecular docking simulations of its interaction with T7 DNA polymerase (a thioredoxin-specific substrate) and comparisons with other known members of the thioredoxin/glutaredoxin family of proteins strongly suggest that MtH895 is more akin to a thioredoxin. Furthermore, measurement of the pK(a) values of its active site thiols along with direct measurements of the thioredoxin/glutaredoxin activity has confirmed that MtH895 is, indeed, a thioredoxin and exhibits no glutaredoxin activity. We have also identified a group of previously unknown proteins from several other archaebacteria that have significant (34-44%) sequence identity with MtH895. These proteins have unusual active site -CXXC- motifs not found in any known thioredoxin or glutaredoxin. On the basis of the results presented here, we predict that these small proteins are all members of a new class of truncated thioredoxins. | As part of a high-throughput, structural proteomic project we have used NMR spectroscopy to determine the solution structure and ascertain the function of a previously unknown, conserved protein (MtH895) from the thermophilic archeon Methanobacterium thermoautotrophicum. Our findings indicate that MtH895 contains a central four-stranded beta-sheet core surrounded by two helices on one side and a third on the other. It has an overall fold superficially similar to that of a glutaredoxin. However, detailed analysis of its three-dimensional structure along with molecular docking simulations of its interaction with T7 DNA polymerase (a thioredoxin-specific substrate) and comparisons with other known members of the thioredoxin/glutaredoxin family of proteins strongly suggest that MtH895 is more akin to a thioredoxin. Furthermore, measurement of the pK(a) values of its active site thiols along with direct measurements of the thioredoxin/glutaredoxin activity has confirmed that MtH895 is, indeed, a thioredoxin and exhibits no glutaredoxin activity. We have also identified a group of previously unknown proteins from several other archaebacteria that have significant (34-44%) sequence identity with MtH895. These proteins have unusual active site -CXXC- motifs not found in any known thioredoxin or glutaredoxin. On the basis of the results presented here, we predict that these small proteins are all members of a new class of truncated thioredoxins. | ||
| - | + | Identification of a novel archaebacterial thioredoxin: determination of function through structure.,Bhattacharyya S, Habibi-Nazhad B, Amegbey G, Slupsky CM, Yee A, Arrowsmith C, Wishart DS Biochemistry. 2002 Apr 16;41(15):4760-70. PMID:11939770<ref>PMID:11939770</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 1ilo" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | + | <references/> | |
| - | [[Category: Bhattacharyya | + | __TOC__ |
| - | [[Category: Habibi-Nazhad | + | </StructureSection> |
| - | + | [[Category: Large Structures]] | |
| - | [[Category: Slupsky | + | [[Category: Methanothermobacter thermautotrophicus str. Delta H]] |
| - | [[Category: Sykes | + | [[Category: Bhattacharyya S]] |
| - | [[Category: Wishart | + | [[Category: Habibi-Nazhad B]] |
| - | + | [[Category: Slupsky CM]] | |
| - | + | [[Category: Sykes BD]] | |
| - | + | [[Category: Wishart DS]] | |
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Current revision
NMR structure of a thioredoxin, MtH895, from the archeon Methanobacterium thermoautotrophicum strain delta H.
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