1ilo | pdb_00001ilo

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

spinqualitylabelsall models 1ilo Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ilo is a 1 chain structure with sequence from Methanothermobacter thermautotrophicus str. Delta H. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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