4Q37
Crystal structure of the hypothetical protein TM0182 Thermotoga maritima, N-terminal domain.
Summary for 4Q37
| Entry DOI | 10.2210/pdb4q37/pdb |
| Descriptor | Radical SAM protein, PLATINUM (II) ION (3 entities in total) |
| Functional Keywords | alpha-beta fold, unknown function |
| Biological source | Thermotoga maritima |
| Total number of polymer chains | 6 |
| Total formula weight | 90259.34 |
| Authors | Hocker, B.,Farias-Rico, J.A. (deposition date: 2014-04-11, release date: 2014-07-16, Last modification date: 2024-02-28) |
| Primary citation | Farias-Rico, J.A.,Schmidt, S.,Hocker, B. Evolutionary relationship of two ancient protein superfolds. Nat.Chem.Biol., 10:710-715, 2014 Cited by PubMed Abstract: Proteins are the molecular machines of the cell that fold into specific three-dimensional structures to fulfill their functions. To improve our understanding of how the structure and function of proteins arises, it is crucial to understand how evolution has generated the structural diversity we observe today. Classically, proteins that adopt different folds are considered to be nonhomologous. However, using state-of-the-art tools for homology detection, we found evidence of homology between proteins of two ancient and highly populated protein folds, the (βα)8-barrel and the flavodoxin-like fold. We detected a family of sequences that show intermediate features between both folds and determined what is to our knowledge the first representative crystal structure of one of its members, giving new insights into the evolutionary link of two of the earliest folds. Our findings contribute to an emergent vision where protein superfolds share common ancestry and encourage further approaches to complete the mapping of structure space onto sequence space. PubMed: 25038785DOI: 10.1038/nchembio.1579 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.19 Å) |
Structure validation
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