6TH8
Reconstructing the Origins of the HemD-like fold
Summary for 6TH8
Entry DOI | 10.2210/pdb6th8/pdb |
NMR Information | BMRB: 34452 |
Descriptor | cU3Sd (1 entity in total) |
Functional Keywords | protein design, hemd-like fold, flavodoxin-like fold, flavoprotein |
Biological source | Thermus thermophilus |
Total number of polymer chains | 1 |
Total formula weight | 13651.65 |
Authors | Coles, M.,Toledo-Patino, S.,Chaubey, M.,Hocker, B. (deposition date: 2019-11-19, release date: 2019-11-27, Last modification date: 2024-06-19) |
Primary citation | Toledo-Patino, S.,Chaubey, M.,Coles, M.,Hocker, B. Reconstructing the Remote Origins of a Fold Singleton from a Flavodoxin-Like Ancestor. Biochemistry, 58:4790-4793, 2019 Cited by PubMed Abstract: Evolutionary processes that led to the emergence of structured protein domains left footprints in the sequences of modern proteins. We searched for such hints employing state-of-the-art sequence analysis and found evidence that the HemD-like fold emerged from the flavodoxin-like fold through segment swap and gene duplication. To verify this hypothesis, we reverted these evolutionary steps experimentally, constructing a HemD-half that resulted in a protein with the canonical flavodoxin-like architecture. These results of fold reconstruction from the sequence of a different fold strongly support our hypothesis of common ancestry. It further illustrates the plasticity of modern proteins to form new folded proteins. PubMed: 31724394DOI: 10.1021/acs.biochem.9b00900 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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