1ilo

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[[Image:1ilo.png|left|200px]]
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==NMR structure of a thioredoxin, MtH895, from the archeon Methanobacterium thermoautotrophicum strain delta H.==
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<StructureSection load='1ilo' size='340' side='right' caption='[[1ilo]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ilo]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ILO FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MtH895 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=187420 Methanothermobacter thermautotrophicus str. Delta H])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoadenylyl-sulfate_reductase_(thioredoxin) Phosphoadenylyl-sulfate reductase (thioredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.8 1.8.4.8] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ilo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ilo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ilo RCSB], [http://www.ebi.ac.uk/pdbsum/1ilo PDBsum], [http://www.topsan.org/Proteins/NESGC/1ilo TOPSAN]</span></td></tr>
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<table>
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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/il/1ilo_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/chain_selection.php?pdb_ID=2ata 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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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.
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{{STRUCTURE_1ilo| PDB=1ilo | SCENE= }}
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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>
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===NMR structure of a thioredoxin, MtH895, from the archeon Methanobacterium thermoautotrophicum strain delta H.===
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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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{{ABSTRACT_PUBMED_11939770}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1ilo]] is a 1 chain structure with sequence from [http://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].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:011939770</ref><ref group="xtra">PMID:011854485</ref><references group="xtra"/>
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[[Category: Methanothermobacter thermautotrophicus str. delta h]]
[[Category: Methanothermobacter thermautotrophicus str. delta h]]
[[Category: Bhattacharyya, S.]]
[[Category: Bhattacharyya, S.]]

Revision as of 12:24, 28 September 2014

NMR structure of a thioredoxin, MtH895, from the archeon Methanobacterium thermoautotrophicum strain delta H.

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