1EIW
Solution structure of hypothetical protein MTH538 from Methanobacterium thermoautotrophicum
Summary for 1EIW
| Entry DOI | 10.2210/pdb1eiw/pdb |
| Descriptor | HYPOTHETICAL PROTEIN MTH538 (1 entity in total) |
| Functional Keywords | chey-like fold, flavodoxin-like fold, (a/b)5 doubly wound fold, parallel beta sheet, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg |
| Biological source | Methanothermobacter thermautotrophicus |
| Total number of polymer chains | 1 |
| Total formula weight | 12395.94 |
| Authors | Cort, J.R.,Arrowsmith, C.H.,Kennedy, M.A.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2000-02-29, release date: 2000-09-06, Last modification date: 2024-05-22) |
| Primary citation | Cort, J.R.,Yee, A.,Edwards, A.M.,Arrowsmith, C.H.,Kennedy, M.A. Structure-based functional classification of hypothetical protein MTH538 from Methanobacterium thermoautotrophicum. J.Mol.Biol., 302:189-203, 2000 Cited by PubMed Abstract: The structure of MTH538, a previously uncharacterized hypothetical protein from Methanobacterium thermoautotrophicum, has been determined by NMR spectroscopy. MTH538 is one of numerous structural genomics targets selected in a genome-wide survey of uncharacterized sequences from this organism. MTH538 is a so-called singleton, a sequence not closely related to any other (known) sequences. The structure of MTH538 closely resembles the known structures of receiver domains from two component response regulator systems, such as CheY, and is similar to the structures of flavodoxins and GTP-binding proteins. Tests on MTH538 for characteristic activities of CheY and flavodoxin were negative. MTH538 did not become phosphorylated in the presence of acetyl phosphate and Mg(2+), although it appeared to bind Mg(2+). MTH538 also did not bind flavin mononucleotide (FMN) or coenzyme F(420). Nevertheless, sequence and structure parallels between MTH538/CheY and two families of ATPase/phosphatase proteins suggest that MTH538 may have a role in a phosphorylation-independent two-component response regulator system. PubMed: 10964569DOI: 10.1006/jmbi.2000.4052 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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