1PU1
Solution structure of the Hypothetical protein mth677 from Methanothermobacter Thermautotrophicus
Summary for 1PU1
| Entry DOI | 10.2210/pdb1pu1/pdb |
| Descriptor | Hypothetical protein MTH677 (1 entity in total) |
| Functional Keywords | structural genomics, alpha and beta protein (a+b), unknown function |
| Biological source | Methanothermobacter thermautotrophicus |
| Total number of polymer chains | 1 |
| Total formula weight | 10534.65 |
| Authors | Blanco, F.J.,Yee, A.,Campos-Olivas, R.,Devos, D.,Valencia, A.,Arrowsmith, C.H.,Rico, M. (deposition date: 2003-06-23, release date: 2004-06-08, Last modification date: 2024-05-22) |
| Primary citation | Blanco, F.J.,Yee, A.,Campos-Olivas, R.,Ortiz, A.R.,Devos, D.,Valencia, A.,Arrowsmith, C.H.,Rico, M. Solution structure of the hypothetical protein Mth677 from Methanobacterium thermoautotrophicum: A novel {alpha}+{beta} fold Protein Sci., 13:1458-1465, 2004 Cited by PubMed Abstract: The structure of Mth677, a hypothetical protein from Methanobacterium thermoautotrophicum (Mth), has been determined by using heteronuclear nuclear magnetic resonance (NMR) methods on a double-labeled (15)N-(13)C sample. Mth677 adopts a novel alpha+beta fold, consisting of two alpha-helices (one N terminal and one C terminal) packed on the same side of a central beta-hairpin. This structure is likely shared by its three orthologs, detected in three other Archaebacteria. There are no clear features in the sequences of these proteins or in the genome organization of Mth to make a reliable functional assignment to this protein. However, the structural similarity to Escherichia coli MinE, the protein which controls that division occurs at the midcell site, lends support to the proposal that Mth677 might be, in Mth, the counterpart of the topological specificity domain of MinE in E. coli. PubMed: 15152082DOI: 10.1110/ps.04620504 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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