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| | ==NMR structure of a thioredoxin, MtH895, from the archeon Methanobacterium thermoautotrophicum strain delta H.== | | ==NMR structure of a thioredoxin, MtH895, from the archeon Methanobacterium thermoautotrophicum strain delta H.== |
| - | <StructureSection load='1ilo' size='340' side='right'caption='[[1ilo]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | + | <StructureSection load='1ilo' size='340' side='right'caption='[[1ilo]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ilo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Metth Metth]. 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> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MtH895 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=187420 METTH])</td></tr> | + | </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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoadenylyl-sulfate_reductase_(thioredoxin) Phosphoadenylyl-sulfate reductase (thioredoxin)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.8 1.8.4.8] </span></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> | | <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> | | </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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Metth]] | + | [[Category: Methanothermobacter thermautotrophicus str. Delta H]] |
| - | [[Category: Bhattacharyya, S]] | + | [[Category: Bhattacharyya S]] |
| - | [[Category: Habibi-Nazhad, B]] | + | [[Category: Habibi-Nazhad B]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Slupsky CM]] |
| - | [[Category: Slupsky, C M]] | + | [[Category: Sykes BD]] |
| - | [[Category: Sykes, B D]] | + | [[Category: Wishart DS]] |
| - | [[Category: Wishart, D S]] | + | |
| - | [[Category: Beta-alpha-beta-alpha-beta-beta-alpha motif]]
| + | |
| - | [[Category: Nesg]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| Structural highlights
Function
THIRX_METTH Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase. Has low thioredoxin activity in vitro.[1]
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 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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bhattacharyya S, Habibi-Nazhad B, Amegbey G, Slupsky CM, Yee A, Arrowsmith C, Wishart DS. Identification of a novel archaebacterial thioredoxin: determination of function through structure. Biochemistry. 2002 Apr 16;41(15):4760-70. PMID:11939770
- ↑ Bhattacharyya S, Habibi-Nazhad B, Amegbey G, Slupsky CM, Yee A, Arrowsmith C, Wishart DS. Identification of a novel archaebacterial thioredoxin: determination of function through structure. Biochemistry. 2002 Apr 16;41(15):4760-70. PMID:11939770
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