1ilo: Difference between revisions

<StructureSection load='1ilo' size='340' side='right'caption='[[1ilo]]' scene=''>

<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>

<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>

[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>

    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/1ilo_consurf.spt"</scriptWhenChecked>

    <text>to colour the structure by Evolutionary Conservation</text>

</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].

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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

<div class="pdbe-citations 1ilo" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Large Structures]]

[[Category: Methanothermobacter thermautotrophicus str. Delta H]]

[[Category: Bhattacharyya S]]

[[Category: Habibi-Nazhad B]]

[[Category: Slupsky CM]]

[[Category: Sykes BD]]

[[Category: Wishart DS]]