1ILO
NMR structure of a thioredoxin, MtH895, from the archeon Methanobacterium thermoautotrophicum strain delta H.
Summary for 1ILO
| Entry DOI | 10.2210/pdb1ilo/pdb |
| NMR Information | BMRB: 4991 |
| Descriptor | conserved hypothetical protein MtH895 (1 entity in total) |
| Functional Keywords | beta-alpha-beta-alpha-beta-beta-alpha motif, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg |
| Biological source | Methanothermobacter thermautotrophicus str. Delta H |
| Total number of polymer chains | 1 |
| Total formula weight | 8466.00 |
| Authors | Bhattacharyya, S.,Habibi-Nazhad, B.,Slupsky, C.M.,Sykes, B.D.,Wishart, D.S.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2001-05-08, release date: 2001-11-14, Last modification date: 2024-05-22) |
| Primary citation | Bhattacharyya, S.,Habibi-Nazhad, B.,Amegbey, G.,Slupsky, C.M.,Yee, A.,Arrowsmith, C.,Wishart, D.S. Identification of a novel archaebacterial thioredoxin: determination of function through structure. Biochemistry, 41:4760-4770, 2002 Cited by PubMed Abstract: 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. PubMed: 11939770DOI: 10.1021/bi0115176 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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