|Protein Science (2004) 13(6):1458-65|
|Northeast Structural Genomics Consortium|
(click to unfold)
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.
|chemistry genetics metabolism |
|Models, Molecular Archaeal Proteins Molecular Sequence Data Protein Conformation Methanobacterium Cloning, Molecular Protein Folding Amino Acid Sequence Nuclear Magnetic Resonance, Biomolecular Structural Homology, Protein Solutions |
|1 (Last update: 04/21/2018 1:04:17pm)|
|Protein Sci. 2004 Jun;13(6):1458-65.|